Download MendeleyThe Crystal structure of SpoVG from Staphylococcus epidermidis ATCC 12228
Tan, K., Maltseva, N., Bargassa, M., Joachimiak, A.To be published.
2I9Z | pdb_00002i9z
Structural Genomics, the Crystal structure of full-length SpoVG from Staphylococcus epidermidis ATCC 12228
- PDB DOI: https://doi.org/10.2210/pdb2I9Z/pdb
- Classification: STRUCTURAL GENOMICS, UNKNOWN FUNCTION
- Organism(s): Staphylococcus epidermidis ATCC 12228
- Expression System: Escherichia coli BL21
- Mutation(s): Yes
- Deposited: 2006-09-06 Released: 2006-10-10
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.30 Å
- R-Value Free: 0.264 (Depositor), 0.230 (DCC)
- R-Value Work: 0.223 (Depositor), 0.220 (DCC)
- R-Value Observed: 0.225 (Depositor)
Starting Model: experimental
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wwPDB Validation 3D Report Full Report
This is version 1.5 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 septation protein spoVG | 105 | Staphylococcus epidermidis ATCC 12228 | Mutation(s): 5 Gene Names: spoVG, SE_2285 |  | |
UniProt | |||||
Find proteins for Q8CML1 (Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200)) Explore Q8CML1 Go to UniProtKB: Q8CML1 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q8CML1 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| EDO Query on EDO | C [auth A], D [auth A], E [auth B], F [auth B] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-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: 2.30 Å
- R-Value Free: 0.264 (Depositor), 0.230 (DCC)
- R-Value Work: 0.223 (Depositor), 0.220 (DCC)
- R-Value Observed: 0.225 (Depositor)
Space Group: P 41 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 63.604 | α = 90 |
| b = 63.604 | β = 90 |
| c = 98.498 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| SBC-Collect | data collection |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| MOLREP | phasing |
Entry History
Deposition Data
- Released Date: 2006-10-10 Deposition Author(s): Tan, K., Maltseva, N., Bargassa, M., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2006-10-10
Type: Initial release - Version 1.1: 2007-10-16
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Derived calculations, Source and taxonomy, Version format compliance - Version 1.3: 2023-08-30
Changes: Data collection, Database references, Derived calculations, Refinement description - Version 1.4: 2023-11-15
Changes: Data collection - Version 1.5: 2024-10-30
Changes: Structure summary
