Download MendeleyNon-catalytic-Region Mutations Conferring Transition of Class A beta-Lactamases Into ESBLs.
Cao, T.-P., Yi, H., Dhanasingh, I., Ghosh, S., Choi, J.M., Lee, K.H., Ryu, S., Kim, H.S., Lee, S.H.(2020) Front Mol Biosci
6AFN | pdb_00006afn
Crystal structure of class A b-lactamase, PenL, variant Cys69Tyr, from Burkholderia thailandensis, in complex with ceftazidime-like boronic acid
- PDB DOI: https://doi.org/10.2210/pdb6AFN/pdb
- Classification: HYDROLASE
- Organism(s): Burkholderia thailandensis
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2018-08-08 Released: 2020-01-15
- Funding Organization(s): National Research Foundation (Korea)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.40 ?
- R-Value Free: 0.170 (Depositor), 0.170 (DCC)
- R-Value Work: 0.147 (Depositor), 0.150 (DCC)
- R-Value Observed: 0.148 (Depositor)
Starting Model: experimental
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This is version 1.4 of the entry. See complete history.
Literature
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Beta-lactamase | 268 | Burkholderia thailandensis | Mutation(s): 1 Gene Names: A8H35_31635 EC: 3.5.2.6 |  | |
UniProt | |||||
Find proteins for Q2T5A3 (Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264)) Explore Q2T5A3 Go to UniProtKB: Q2T5A3 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q2T5A3 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| CB4 Query on CB4 | B [auth A] | PINACOL[[2-AMINO-ALPHA-(1-CARBOXY-1-METHYLETHOXYIMINO)-4-THIAZOLEACETYL]AMINO]METHANEBORONATE C10 H15 B N4 O6 S ZECCQELUYUPTSB-UUASQNMZSA-N |  | ||
| GOL Query on GOL | C [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.40 ?
- R-Value Free: 0.170 (Depositor), 0.170 (DCC)
- R-Value Work: 0.147 (Depositor), 0.150 (DCC)
- R-Value Observed: 0.148 (Depositor)
Space Group: P 21 21 21
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 38.66 | α = 90 |
| b = 53.238 | β = 90 |
| c = 122.981 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| MOLREP | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2020-01-15 Deposition Author(s): Cao, T.-P., Choi, J.M., Lee, S.H.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Research Foundation (Korea) | Korea, Republic Of | NRF-2016R1D1A1B03932717 |
Revision History (Full details and data files)
- Version 1.0: 2020-01-15
Type: Initial release - Version 1.1: 2020-02-19
Changes: Database references, Source and taxonomy, Structure summary - Version 1.2: 2020-12-09
Changes: Database references - Version 1.3: 2023-11-22
Changes: Data collection, Database references, Refinement description - Version 1.4: 2024-11-20
Changes: Structure summary
