5G05 | pdb_00005g05

Cryo-EM structure of combined apo phosphorylated APC


Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
BSCOP2B SuperfamilyRING/U-box like 8082719 3000160 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyTPR-like 8057064 3001345 SCOP2B (2022-06-29)
PSCOP2B SuperfamilyTPR-like 8057064 3001345 SCOP2B (2022-06-29)
ESCOP2B SuperfamilyAnaphase-promoting complex subunit 16-like 8053719 3002218 SCOP2B (2022-06-29)
LSCOP2B Superfamilygalactose-binding domain-like 8037020 3000087 SCOP2B (2022-06-29)
MSCOP2 FamilyAnaphase-promoting complex subunit 13 8047611 4005717 SCOP2 (2022-06-29)
MSCOP2 SuperfamilyAnaphase-promoting complex subunit 13 8093173 3002688 SCOP2 (2022-06-29)
GSCOP2B SuperfamilyCDC26-like 8053843 3002235 SCOP2B (2022-06-29)
R [auth W]SCOP2B SuperfamilyCDC26-like 8053843 3002235 SCOP2B (2022-06-29)
ISCOP2B SuperfamilyWD40 repeat-like 8106386 3001694 SCOP2B (2022-06-29)
ISCOP2B SuperfamilyWD40 repeat-like 8106386 3001694 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
Bzf-rbx1e5g05B1 A: few secondary structure elementsX: RING/U-box-likeH: RING/U-box-likeT: RING/U-boxF: zf-rbx1ECOD (1.6)
CKOG1155e5g05C2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: KOG1155ECOD (1.6)
CANAPC8e5g05C1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: ANAPC8ECOD (1.6)
PKOG1155e5g05P3 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: KOG1155ECOD (1.6)
PANAPC8e5g05P2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: ANAPC8ECOD (1.6)
HTPR_11_7e5g05H1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: TPR_11_7ECOD (1.6)
FTPR_11_7e5g05F1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: TPR_11_7ECOD (1.6)
LANAPC10e5g05L1 A: beta sandwichesX: jelly-rollH: Concanavalin A-likeT: Galactose-binding domain-likeF: ANAPC10ECOD (1.6)
NCullin_4the5g05N3 A: alpha arraysX: HTHH: HTHT: wingedF: Cullin_4thECOD (1.6)
NCullin_2nde5g05N4 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: Cullin_2ndECOD (1.6)
NKOG2165e5g05N2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: KOG2165ECOD (1.6)
NCullin_3rde5g05N1 A: a+b duplicates or obligate multimersX: a+b domain in cullin-like proteins (From Topology)H: a+b domain in cullin-like proteins (From Topology)T: a+b domain in cullin-like proteinsF: Cullin_3rdECOD (1.6)
OApc5_Ne5g05O2 A: alpha arraysX: SHQ1 C-terminal domain-likeH: Anaphase-promoting complex subunit 5 N-terminal domain (From Topology)T: Anaphase-promoting complex subunit 5 N-terminal domainF: Apc5_NECOD (1.6)
OANAPC5e5g05O1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: ANAPC5ECOD (1.6)
AKOG1858_3rde5g05A5 A: beta sandwichesX: 26S proteasome subunit Rpn2 C-terminal domain (From Topology)H: 26S proteasome subunit Rpn2 C-terminal domain (From Topology)T: 26S proteasome subunit Rpn2 C-terminal domainF: KOG1858_3rdECOD (1.6)
AANAPC1e5g05A3 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: ANAPC1ECOD (1.6)
AKOG1858_2nde5g05A1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Proteasome/cyclosome (PC) repeat (From Topology)T: Proteasome/cyclosome (PC) repeatF: KOG1858_2ndECOD (1.6)
AKOG1858_1ste5g05A2 A: alpha superhelicesX: Repetitive alpha hairpinsH: Anaphase-promoting complex subunit 1 first helical domain (From Topology)T: Anaphase-promoting complex subunit 1 first helical domainF: KOG1858_1stECOD (1.6)
AKOG1858_4the5g05A4 A: alpha superhelicesX: Repetitive alpha hairpinsH: Anaphase-promoting complex subunit 1 second helical domain (From Topology)T: Anaphase-promoting complex subunit 1 second helical domainF: KOG1858_4thECOD (1.6)
S [auth X]TPR_19,ANAPC8e5g05X1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: TPR_19,ANAPC8ECOD (1.6)
T [auth Y]TPR_11_9e5g05Y1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: TPR_11_9ECOD (1.6)
IANAPC4_WD40e5g05I2 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: ANAPC4_WD40ECOD (1.6)
IANAPC4e5g05I1 A: alpha bundlesX: Four-helical up-and-down bundleH: Helical bundle domain in anaphase-promoting complex subunit 4 (From Topology)T: Helical bundle domain in anaphase-promoting complex subunit 4F: ANAPC4ECOD (1.6)
JTPR_11_7e5g05J1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: TPR_11_7ECOD (1.6)
KTPR_11_7e5g05K1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: TPR_11_7ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF12861Anaphase-promoting complex subunit 11 RING-H2 finger (zf-ANAPC11)Anaphase-promoting complex subunit 11 RING-H2 fingerApc11 is one of the subunits of the anaphase-promoting complex or cyclosome [1]. The APC subunits are cullin family proteins with ubiquitin ligase activity [2]. Polyubiquitination marks proteins for degradation by the 26S proteasome and is carried ou ...Apc11 is one of the subunits of the anaphase-promoting complex or cyclosome [1]. The APC subunits are cullin family proteins with ubiquitin ligase activity [2]. Polyubiquitination marks proteins for degradation by the 26S proteasome and is carried out by a cascade of enzymes that includes ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s), and ubiquitin ligases (E3s). Apc11 acts as an E3 enzyme and is responsible for recruiting E2s to the APC and for mediating the subsequent transfer of ubiquitin to APC substrates in vivo. In Saccharomyces cerevisiae this RING-H2 finger protein defines the minimal ubiquitin ligase activity of the APC, and the integrity of the RING-H2 finger is essential for budding yeast cell viability [3].
Domain
C, P
PF04049Anaphase promoting complex subunit 8 / Cdc23 (ANAPC8)Anaphase promoting complex subunit 8 / Cdc23- Repeat
F, H
PF12895Anaphase-promoting complex, cyclosome, subunit 3 (ANAPC3)Anaphase-promoting complex, cyclosome, subunit 3- Repeat
F, H
PF00515Tetratricopeptide repeat (TPR_1)Tetratricopeptide repeat- Repeat
PF03256Anaphase-promoting complex, subunit 10 (APC10) (ANAPC10)Anaphase-promoting complex, subunit 10 (APC10)- Family
PF12862Anaphase-promoting complex subunit 5 (ANAPC5)Anaphase-promoting complex subunit 5- Repeat
PF21371Anaphase-promoting complex subunit 5, N-terminal domain (Apc5_N)Anaphase-promoting complex subunit 5, N-terminal domainThis domain is found at the N-terminal end of Anaphase-promoting complex subunit 5 from humans (Apc5), a component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitos ...This domain is found at the N-terminal end of Anaphase-promoting complex subunit 5 from humans (Apc5), a component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. This domain has an alpha-helical fold [1-4]. It is normally found in association with Pfam:PF12862.
Domain
PF20518Anaphase-promoting complex subunit 1 middle domain (Apc1_MidN)Anaphase-promoting complex subunit 1 middle domain- Repeat
PF18122Anaphase-promoting complex sub unit 1 C-terminal domain (APC1_C)Anaphase-promoting complex sub unit 1 C-terminal domainThis is the C-terminal domain of chain A, also known as sub-unit 1, found in anaphase-promoting complex (APC/C) present in Homo sapiens. APC/C is an ubiquitin ligase that controls chromosome segregation and mitotic exit [1]. Domain
PF21282APC1 beta sandwich domain (APC1_3rd)APC1 beta sandwich domainThis domain is found close to the C-terminus of the APC1 protein which is a component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the ce ...This domain is found close to the C-terminus of the APC1 protein which is a component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle.
Domain
PF05839Apc13p protein (Apc13p)Apc13p protein- Family
S [auth X],
T [auth Y]
PF13181Tetratricopeptide repeat (TPR_8)Tetratricopeptide repeat- Repeat
S [auth X],
T [auth Y]
PF13432Tetratricopeptide repeat (TPR_16)Tetratricopeptide repeat- Repeat
PF15243Anaphase-promoting complex subunit 15 (ANAPC15)Anaphase-promoting complex subunit 15- Family
G,
R [auth W]
PF10471Anaphase-promoting complex APC subunit CDC26 (ANAPC_CDC26)Anaphase-promoting complex APC subunit CDC26- Family
PF12896Anaphase-promoting complex, cyclosome, subunit 4 (ANAPC4)Anaphase-promoting complex, cyclosome, subunit 4Apc4 is one of the larger of the subunits of the anaphase-promoting complex or cyclosome. This family represents the long domain downstream of the WD40 repeat/s that are present on the Apc4 subunits. The anaphase-promoting complex is a multiprotein s ...Apc4 is one of the larger of the subunits of the anaphase-promoting complex or cyclosome. This family represents the long domain downstream of the WD40 repeat/s that are present on the Apc4 subunits. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes [1,2]. Results in C.elegans show that the primary essential role of the spindle assembly checkpoint is not in the chromosome segregation process itself but rather in delaying anaphase onset until all chromosomes are properly attached to the spindle. the APC/C is likely to be required for all metaphase-to-anaphase transitions in a multicellular organism [3].
Domain
PF12894Anaphase-promoting complex subunit 4 WD40 domain (ANAPC4_WD40)Anaphase-promoting complex subunit 4 WD40 domain- Repeat
J, K
PF12895Anaphase-promoting complex, cyclosome, subunit 3 (ANAPC3)Anaphase-promoting complex, cyclosome, subunit 3- Repeat
J, K
PF13424Tetratricopeptide repeat (TPR_12)Tetratricopeptide repeat- Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
ANAPHASE-PROMOTING COMPLEX SUBUNIT 11
C, P
CELL DIVISION CYCLE PROTEIN 23 HOMOLOG
ANAPHASE-PROMOTING COMPLEX SUBUNIT 16-
F, H
CELL DIVISION CYCLE PROTEIN 27 HOMOLOG
ANAPHASE-PROMOTING COMPLEX SUBUNIT 10-
ANAPHASE-PROMOTING COMPLEX SUBUNIT 2
ANAPHASE-PROMOTING COMPLEX SUBUNIT 5
Q [auth T]UNIDENTIFIED PEPTIDE---
ANAPHASE-PROMOTING COMPLEX SUBUNIT 1
ANAPHASE-PROMOTING COMPLEX SUBUNIT 13-
S [auth X],
T [auth Y]
ANAPHASE-PROMOTING COMPLEX SUBUNIT 7
ANAPHASE-PROMOTING COMPLEX SUBUNIT 15-
G,
R [auth W]
ANAPHASE-PROMOTING COMPLEX SUBUNIT CDC26-
ANAPHASE-PROMOTING COMPLEX SUBUNIT 4
J, K
CELL DIVISION CYCLE PROTEIN 16 HOMOLOG-

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
IPR051031RING-box E3 Ubiquitin LigaseFamily
IPR013083Zinc finger, RING/FYVE/PHD-typeHomologous Superfamily
IPR024991Anaphase-promoting complex subunit 11, RING-H2 fingerDomain
IPR001841Zinc finger, RING-typeDomain
C, P
IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
C, P
IPR007192Cdc23Domain
C, P
IPR019734Tetratricopeptide repeatRepeat
IPR029641Anaphase-promoting complex subunit 16Family
F, H
IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
F, H
IPR019734Tetratricopeptide repeatRepeat
IPR016901Anaphase-promoting complex subunit APC10/Doc1Family
IPR008979Galactose-binding-like domain superfamilyHomologous Superfamily
IPR004939APC10/DOC domainDomain
IPR014786Anaphase-promoting complex subunit 2, C-terminalDomain
IPR016158Cullin homology domainDomain
IPR001373Cullin, N-terminalDomain
IPR036388Winged helix-like DNA-binding domain superfamilyHomologous Superfamily
IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
IPR036317Cullin homology domain superfamilyHomologous Superfamily
IPR044554Anaphase-promoting complex subunit 2Family
IPR026000Anaphase-promoting complex subunit 5 domainDomain
IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
IPR037679Anaphase-promoting complex subunit 5Family
IPR019734Tetratricopeptide repeatRepeat
IPR048968Anaphase-promoting complex subunit 5, N-terminal domainDomain
IPR041221Anaphase-promoting complex subunit 1, C-terminalDomain
IPR046794Anaphase-promoting complex subunit 1, middle domainDomain
IPR024990Anaphase-promoting complex subunit 1Family
IPR048971Anaphase-promoting complex subunit 1, beta-sandwich domainDomain
IPR049255Anaphase-promoting complex subunit 1, N-terminal domainDomain
IPR011989Armadillo-like helicalHomologous Superfamily
IPR008401Apc13Family
S [auth X],
T [auth Y]
IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
S [auth X],
T [auth Y]
IPR019734Tetratricopeptide repeatRepeat
IPR026182Anaphase-promoting complex subunit 15Family
G,
R [auth W]
IPR018860Anaphase-promoting complex, subunit CDC26Family
IPR017169Anaphase-promoting complex subunit 4, metazoaFamily
IPR024977Anaphase-promoting complex subunit 4-like, WD40 domainDomain
IPR036322WD40-repeat-containing domain superfamilyHomologous Superfamily
IPR024789Anaphase-promoting complex subunit 4Family
IPR024790Anaphase-promoting complex subunit 4, long domainDomain
IPR015943WD40/YVTN repeat-like-containing domain superfamilyHomologous Superfamily
IPR056358Anaphase-promoting complex subunit 4, C-terminal half WD40 domainDomain
J, K
IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
J, K
IPR019734Tetratricopeptide repeatRepeat

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
PharosQ9NYG5
C, P
PharosQ9UJX2
PharosQ96DE5
F, H
PharosP30260
PharosQ9UM13
PharosQ9UJX6
PharosQ9UJX4
PharosQ9H1A4
S [auth X],
T [auth Y]
PharosQ9UJX3
PharosP60006
G,
R [auth W]
PharosQ8NHZ8
PharosQ9UJX5
J, K
PharosQ13042
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