6R1B | pdb_00006r1b

Crystal structure of UgpB from Mycobacterium tuberculosis in complex with glycerophosphocholine

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	SBP_bac_1_N_1	e6r1bA1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_1_N_1	ECOD (1.6)
A	SBP_bac_1_C_1	e6r1bA2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_1_C_1	ECOD (1.6)
B	SBP_bac_1_N_1	e6r1bB1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_1_N_1	ECOD (1.6)
B	SBP_bac_1_C_1	e6r1bB2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_1_C_1	ECOD (1.6)
C	SBP_bac_1_N_1	e6r1bC1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_1_N_1	ECOD (1.6)
C	SBP_bac_1_C_1	e6r1bC2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_1_C_1	ECOD (1.6)
D	SBP_bac_1_N_1	e6r1bD2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_1_N_1	ECOD (1.6)
D	SBP_bac_1_C_1	e6r1bD1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_1_C_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (utative)
B	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (utative)
C	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (utative)
D	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01547	Bacterial extracellular solute-binding protein (SBP_bac_1)	Bacterial extracellular solute-binding protein	-	Family
B	PF01547	Bacterial extracellular solute-binding protein (SBP_bac_1)	Bacterial extracellular solute-binding protein	-	Family
C	PF01547	Bacterial extracellular solute-binding protein (SBP_bac_1)	Bacterial extracellular solute-binding protein	-	Family
D	PF01547	Bacterial extracellular solute-binding protein (SBP_bac_1)	Bacterial extracellular solute-binding protein	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Putative Sn-glycerol-3-phosphate-binding lipoprotein UgpB	cation binding ion binding binding metal ion binding small molecule binding	-	cell periphery cellular anatomical structure plasma membrane membrane
B	Putative Sn-glycerol-3-phosphate-binding lipoprotein UgpB	cation binding ion binding binding metal ion binding small molecule binding	-	cell periphery cellular anatomical structure plasma membrane membrane
C	Putative Sn-glycerol-3-phosphate-binding lipoprotein UgpB	cation binding ion binding binding metal ion binding small molecule binding	-	cell periphery cellular anatomical structure plasma membrane membrane
D	Putative Sn-glycerol-3-phosphate-binding lipoprotein UgpB	cation binding ion binding binding metal ion binding small molecule binding	-	cell periphery cellular anatomical structure plasma membrane membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR050490	Bacterial solute-binding protein 1	Family
A	IPR006311	Twin-arginine translocation pathway, signal sequence	Conserved Site
A	IPR006059	Bacterial-type extracellular solute-binding protein	Family
B	IPR050490	Bacterial solute-binding protein 1	Family
B	IPR006311	Twin-arginine translocation pathway, signal sequence	Conserved Site
B	IPR006059	Bacterial-type extracellular solute-binding protein	Family
C	IPR050490	Bacterial solute-binding protein 1	Family
C	IPR006311	Twin-arginine translocation pathway, signal sequence	Conserved Site
C	IPR006059	Bacterial-type extracellular solute-binding protein	Family
D	IPR050490	Bacterial solute-binding protein 1	Family
D	IPR006311	Twin-arginine translocation pathway, signal sequence	Conserved Site
D	IPR006059	Bacterial-type extracellular solute-binding protein	Family

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A	MLZ	Parent Component: LYS RESID: AA0076 PSI-MOD : N6-methyl-L-lysine MOD:00085
B	MLZ	Parent Component: LYS RESID: AA0076 , AA0076 PSI-MOD : N6-methyl-L-lysine MOD:00085 , N6-methyl-L-lysine MOD:00085
C	MLZ	Parent Component: LYS RESID: AA0076 , AA0076 , AA0076 PSI-MOD : N6-methyl-L-lysine MOD:00085 , N6-methyl-L-lysine MOD:00085 , N6-methyl-L-lysine MOD:00085
D	MLZ	Parent Component: LYS RESID: AA0076 , AA0076 , AA0076 , AA0076 PSI-MOD : N6-methyl-L-lysine MOD:00085 , N6-methyl-L-lysine MOD:00085 , N6-methyl-L-lysine MOD:00085 , N6-methyl-L-lysine MOD:00085

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.