Download MendeleyThe Crystal Structure of the Putative NAD(P)H-Flavin Oxidoreductase from Streptococcus pyogenes M1 GAS
Kim, Y., Duggan, E., Clancy, S., Joachimiak, A.To be published.
2HAY
The Crystal Structure of the Putative NAD(P)H-Flavin Oxidoreductase from Streptococcus pyogenes M1 GAS
- PDB DOI: https://doi.org/10.2210/pdb2HAY/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Streptococcus pyogenes serotype M1
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2006-06-13 Released: 2006-07-04
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.11 Å
- R-Value Free: 0.232
- R-Value Work: 0.175
- R-Value Observed: 0.180
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 |
| Putative NAD(P)H-flavin oxidoreductase | 224 | Streptococcus pyogenes serotype M1 | Mutation(s): 7 EC: 1 |  | |
UniProt | |||||
Find proteins for Q9A120 (Streptococcus pyogenes serotype M1) Explore Q9A120 Go to UniProtKB: Q9A120 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9A120 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| FMN Query on FMN | F [auth A], I [auth B], J [auth C], M [auth D] | FLAVIN MONONUCLEOTIDE C17 H21 N4 O9 P FVTCRASFADXXNN-SCRDCRAPSA-N |  | ||
| SO4 Query on SO4 | E [auth A], G [auth B], H [auth B], K [auth D], L [auth D] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| 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: 2.11 Å
- R-Value Free: 0.232
- R-Value Work: 0.175
- R-Value Observed: 0.180
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 60.205 | α = 90 |
| b = 91.874 | β = 90 |
| c = 175.693 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| SBC-Collect | data collection |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| HKL-3000 | phasing |
| SHELXE | model building |
| SOLVE | phasing |
| RESOLVE | phasing |
| ARP/wARP | model building |
Entry History
Deposition Data
- Released Date: 2006-07-04 Deposition Author(s): Kim, Y., Duggan, E., Clancy, S., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2006-07-04
Type: Initial release - Version 1.1: 2008-05-01
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Advisory, Refinement description, Version format compliance - Version 1.3: 2024-11-06
Changes: Data collection, Database references, Derived calculations, Structure summary
