Download MendeleyCrystal structure of (np_811990.1) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 2.20 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
2FG9
CRYSTAL STRUCTURE OF A PUTATIVE 5-NITROIMIDAZOLE ANTIBIOTIC RESISTANCE PROTEIN (BT_3078) FROM BACTEROIDES THETAIOTAOMICRON VPI-5482 AT 2.20 A RESOLUTION
- PDB DOI: https://doi.org/10.2210/pdb2FG9/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Bacteroides thetaiotaomicron VPI-5482
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2005-12-21 Released: 2006-01-10
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 Å
- R-Value Free: 0.245
- R-Value Work: 0.223
- R-Value Observed: 0.224
This is version 1.4 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| 5-nitroimidazole antibiotic resistance protein | 178 | Bacteroides thetaiotaomicron VPI-5482 | Mutation(s): 8 Gene Names: np_811990.1 |  | |
UniProt | |||||
Find proteins for Q8A377 (Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)) Explore Q8A377 Go to UniProtKB: Q8A377 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q8A377 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| FAD Query on FAD | C [auth A] | FLAVIN-ADENINE DINUCLEOTIDE C27 H33 N9 O15 P2 VWWQXMAJTJZDQX-UYBVJOGSSA-N |  | ||
| EDO Query on EDO | D [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| NI Query on NI | B [auth A] | NICKEL (II) ION Ni VEQPNABPJHWNSG-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 Å
- R-Value Free: 0.245
- R-Value Work: 0.223
- R-Value Observed: 0.224
- Space Group: I 4 3 2
- Diffraction Data: https://doi.org/10.18430/M32FG9
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 134 | α = 90 |
| b = 134 | β = 90 |
| c = 134 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| XSCALE | data scaling |
| PDB_EXTRACT | data extraction |
| XDS | data reduction |
| SHARP | phasing |
Entry History
Deposition Data
- Released Date: 2006-01-10 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2006-01-10
Type: Initial release - Version 1.1: 2008-05-01
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Advisory, Derived calculations, Source and taxonomy, Version format compliance - Version 1.3: 2017-10-25
Changes: Author supporting evidence - Version 1.4: 2023-01-25
Changes: Database references, Derived calculations
