Download MendeleyThe crystal structure of a conserved functionally unknown protein from Anaerococcus prevotii DSM 20548
Tan, K., Li, H., Bearden, J., Joachimiak, A.To be published.
4GXT
The crystal structure of a conserved functionally unknown protein from Anaerococcus prevotii DSM 20548
- PDB DOI: https://doi.org/10.2210/pdb4GXT/pdb
- Classification: Structural Genomics, Unknown Function
- Organism(s): Anaerococcus prevotii DSM 20548
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2012-09-04 Released: 2012-10-03
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.82 Å
- R-Value Free: 0.223
- R-Value Work: 0.173
- R-Value Observed: 0.176
wwPDB Validation 3D Report Full Report
This is version 1.0 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 |
| a conserved functionally unknown protein | 385 | Anaerococcus prevotii DSM 20548 | Mutation(s): 0 Gene Names: Apre_0094 |  | |
UniProt | |||||
Find proteins for C7RF86 (Anaerococcus prevotii (strain ATCC 9321 / DSM 20548 / JCM 6508 / NCTC 11806 / PC1)) Explore C7RF86 Go to UniProtKB: C7RF86 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | C7RF86 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| SO4 Query on SO4 | B [auth A], C [auth A], D [auth A], E [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| GOL Query on GOL | F [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-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: 1.82 Å
- R-Value Free: 0.223
- R-Value Work: 0.173
- R-Value Observed: 0.176
- Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 49.13 | α = 90 |
| b = 53.226 | β = 95.03 |
| c = 75.849 | γ = 90 |
| Software Name | Purpose |
|---|---|
| SBC-Collect | data collection |
| SHELXD | phasing |
| MLPHARE | phasing |
| DM | model building |
| RESOLVE | model building |
| HKL-3000 | phasing |
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| DM | phasing |
| RESOLVE | phasing |
Entry History
Deposition Data
- Released Date: 2012-10-03 Deposition Author(s): Tan, K., Li, H., Bearden, J., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2012-10-03
Type: Initial release
