Download MendeleyThe structure of a functionally unknown conserved protein from Silicibacter pomeroyi DSS
Tan, K., Tesar, C., Freeman, L., Joachimiak, A.To be published.
3IUS | pdb_00003ius
The structure of a functionally unknown conserved protein from Silicibacter pomeroyi DSS
- PDB DOI: https://doi.org/10.2210/pdb3IUS/pdb
- Classification: structural genomics, unknown function
- Organism(s): Ruegeria pomeroyi DSS-3
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2009-08-31 Released: 2009-10-20
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.66 Å
- R-Value Free: 0.257 (Depositor), 0.244 (DCC)
- R-Value Work: 0.217 (Depositor), 0.209 (DCC)
- R-Value Observed: 0.219 (Depositor)
wwPDB Validation 3D Report Full Report
This is version 1.2 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 |
| uncharacterized conserved protein | 286 | Ruegeria pomeroyi DSS-3 | Mutation(s): 0 Gene Names: Silicibacter pomeroyi, SPO3755 |  | |
UniProt | |||||
Find proteins for Q5LM08 (Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)) Explore Q5LM08 Go to UniProtKB: Q5LM08 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q5LM08 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| EDO Query on EDO | E [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| FMT Query on FMT | C [auth A], D [auth A] | FORMIC ACID C H2 O2 BDAGIHXWWSANSR-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.66 Å
- R-Value Free: 0.257 (Depositor), 0.244 (DCC)
- R-Value Work: 0.217 (Depositor), 0.209 (DCC)
- R-Value Observed: 0.219 (Depositor)
Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 57.736 | α = 90 |
| b = 81.648 | β = 94.65 |
| c = 58.655 | γ = 90 |
| Software Name | Purpose |
|---|---|
| SBC-Collect | data collection |
| SHELXD | phasing |
| MLPHARE | phasing |
| DM | model building |
| ARP | model building |
| WARP | model building |
| HKL-3000 | phasing |
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| DM | phasing |
Entry History
Deposition Data
- Released Date: 2009-10-20 Deposition Author(s): Tan, K., Tesar, C., Freeman, L., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2009-10-20
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2024-11-20
Changes: Data collection, Database references, Derived calculations, Structure summary
