Download MendeleyCrystal structure of a putative outer membrane chaperone (OmpH-like) (CC_1914) from Caulobacter crescentus CB15 at 2.83 A resolution (PSI Community Target, Shapiro)
Joint Center for Structural Genomics (JCSG)To be published.
4KQT
Crystal structure of a putative outer membrane chaperone (OmpH-like) (CC_1914) from Caulobacter crescentus CB15 at 2.83 A resolution (PSI Community Target, Shapiro)
- PDB DOI: https://doi.org/10.2210/pdb4KQT/pdb
- Classification: CHAPERONE
- Organism(s): Caulobacter vibrioides CB15
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2013-05-15 Released: 2013-06-12
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.83 Å
- R-Value Free: 0.245
- R-Value Work: 0.208
- R-Value Observed: 0.210
wwPDB Validation 3D Report Full Report
This is version 1.1 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 outer membrane chaperone (OmpH-like) | 195 | Caulobacter vibrioides CB15 | Mutation(s): 0 Gene Names: CC_1914 |  | |
UniProt | |||||
Find proteins for Q9A712 (Caulobacter vibrioides (strain ATCC 19089 / CB15)) Explore Q9A712 Go to UniProtKB: Q9A712 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9A712 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PGE Query on PGE | D [auth A], E [auth A] | TRIETHYLENE GLYCOL C6 H14 O4 ZIBGPFATKBEMQZ-UHFFFAOYSA-N |  | ||
| PEG Query on PEG | B [auth A], C [auth A] | DI(HYDROXYETHYL)ETHER C4 H10 O3 MTHSVFCYNBDYFN-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: 2.83 Å
- R-Value Free: 0.245
- R-Value Work: 0.208
- R-Value Observed: 0.210
- Space Group: H 3 2
- Diffraction Data: https://doi.org/10.18430/M34KQT
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 109.849 | α = 90 |
| b = 109.849 | β = 90 |
| c = 163.704 | γ = 120 |
| Software Name | Purpose |
|---|---|
| MolProbity | model building |
| PDB_EXTRACT | data extraction |
| SHELX | phasing |
| SHARP | phasing |
| XSCALE | data scaling |
| REFMAC | refinement |
| XDS | data reduction |
| SHELXD | phasing |
Entry History
Deposition Data
- Released Date: 2013-06-12 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2013-06-12
Type: Initial release - Version 1.1: 2017-11-15
Changes: Refinement description
