Download MendeleyCrystal Structure of Fmn-Dependent Azoreductase from Enterococcus faecalis at 2.00 A resolution
Liu, Z.J., Chen, H., Chen, L., Shah, N., Rose, J.P., Wang, B.C.To be published.
2HPV
Crystal structure of FMN-Dependent azoreductase from Enterococcus faecalis
- PDB DOI: https://doi.org/10.2210/pdb2HPV/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Enterococcus faecalis
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2006-07-17 Released: 2006-09-12
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.00 Å
- R-Value Free: 0.250
- R-Value Work: 0.199
- R-Value Observed: 0.202
This is version 1.3 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 |
| FMN-dependent NADH-azoreductase | 208 | Enterococcus faecalis | Mutation(s): 4 Gene Names: azoR, azoA EC: 1.7 |  | |
UniProt | |||||
Find proteins for Q831B2 (Enterococcus faecalis (strain ATCC 700802 / V583)) Explore Q831B2 Go to UniProtKB: Q831B2 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q831B2 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| FMN Query on FMN | E [auth A], F [auth B], G [auth C], H [auth D] | FLAVIN MONONUCLEOTIDE C17 H21 N4 O9 P FVTCRASFADXXNN-SCRDCRAPSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B, C, D | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.00 Å
- R-Value Free: 0.250
- R-Value Work: 0.199
- R-Value Observed: 0.202
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 98.038 | α = 90 |
| b = 99.629 | β = 90 |
| c = 106.737 | γ = 90 |
| Software Name | Purpose |
|---|---|
| Sca2Structure | model building |
| REFMAC | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| SCA2STRUCTURE | phasing |
Entry History
Deposition Data
- Released Date: 2006-09-12 Deposition Author(s): Liu, Z.J., Chen, L., Chen, H., Rose, J., Wang, B.C., Southeast Collaboratory for Structural Genomics (SECSG)
Revision History (Full details and data files)
- Version 1.0: 2006-09-12
Type: Initial release - Version 1.1: 2008-04-29
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Derived calculations, Version format compliance - Version 1.3: 2017-09-13
Changes: Refinement description
