Download MendeleyCrystal Structure of the Nitroreductase Family Protein from Streptococcus pneumoniae TIGR4
Kim, Y., Volkart, L., Abdullah, J., Collart, F., Joachimiak, A.To be published.
2B67 | pdb_00002b67
Crystal structure of the Nitroreductase Family Protein from Streptococcus pneumoniae TIGR4
- PDB DOI: https://doi.org/10.2210/pdb2B67/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Streptococcus pneumoniae TIGR4
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2005-09-30 Released: 2005-11-15
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.05 Å
- R-Value Free: 0.247 (Depositor), 0.247 (DCC)
- R-Value Work: 0.177 (Depositor), 0.176 (DCC)
- R-Value Observed: 0.184 (Depositor)
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 |
| COG0778: Nitroreductase | 204 | Streptococcus pneumoniae TIGR4 | Mutation(s): 3 EC: 1.6.99.3 |  | |
UniProt | |||||
Find proteins for A0A0H2UP38 (Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)) Explore A0A0H2UP38 Go to UniProtKB: A0A0H2UP38 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A0A0H2UP38 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| FMN Query on FMN | E [auth A], G [auth B], H [auth C], I [auth D] | FLAVIN MONONUCLEOTIDE C17 H21 N4 O9 P FVTCRASFADXXNN-SCRDCRAPSA-N |  | ||
| ACY Query on ACY | F [auth A] | ACETIC ACID C2 H4 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-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: 2.05 Å
- R-Value Free: 0.247 (Depositor), 0.247 (DCC)
- R-Value Work: 0.177 (Depositor), 0.176 (DCC)
- R-Value Observed: 0.184 (Depositor)
Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 55.4 | α = 90 |
| b = 80.278 | β = 100.61 |
| c = 103.015 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| SBC-Collect | data collection |
| HKL-2000 | data scaling |
| HKL-3000 | phasing |
| SHELXCD | phasing |
| SHELXD | phasing |
| SHELXE | model building |
| MLPHARE | phasing |
| SOLVE | phasing |
| RESOLVE | phasing |
Entry History
Deposition Data
- Released Date: 2005-11-15 Deposition Author(s): Kim, Y., Volkart, L., Abdullah, J., Collart, F., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2005-11-15
Type: Initial release - Version 1.1: 2008-05-01
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Source and taxonomy, Version format compliance - Version 1.3: 2017-10-11
Changes: Refinement description - Version 1.4: 2024-10-30
Changes: Data collection, Database references, Derived calculations, Structure summary
