Download MendeleyThe role of OleA His285 in substrate coordination of long-chain acyl-CoA
Jensen, M.R., Goblirsch, B.R., Esler, M.A., Christenson, J.K., Mohamed, F.A., Wackett, L.P., Wilmot, C.M.To be published.
6B2U
Crystal structure of Xanthomonas campestris OleA H285N with Cerulenin
- PDB DOI: https://doi.org/10.2210/pdb6B2U/pdb
- Classification: TRANSFERASE
- Organism(s): Xanthomonas campestris pv. campestris str. ATCC 33913
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2017-09-20 Released: 2018-02-28
- Funding Organization(s): National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS), BioTechnology Institute
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.04 ?
- R-Value Free: 0.230
- R-Value Work: 0.179
- R-Value Observed: 0.181
Starting Model: experimental
View more details
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 |
| 3-oxoacyl-[ACP] synthase III | 358 | Xanthomonas campestris pv. campestris str. ATCC 33913 | Mutation(s): 1 Gene Names: fabH, XCC0212 EC: 2.3.3.20 |  | |
UniProt | |||||
Find proteins for Q8PDX2 (Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)) Explore Q8PDX2 Go to UniProtKB: Q8PDX2 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q8PDX2 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| CER Query on CER | C [auth A] | (2S, 3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE C12 H19 N O3 QEPYZBPOTYDXNA-FECJWDPASA-N |  | ||
| MN Query on MN | B [auth A] | MANGANESE (II) ION Mn WAEMQWOKJMHJLA-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.04 ?
- R-Value Free: 0.230
- R-Value Work: 0.179
- R-Value Observed: 0.181
- Space Group: P 32 2 1
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 90.516 | ¦Á = 90 |
| b = 90.516 | ¦Â = 90 |
| c = 69.793 | ¦Ă = 120 |
| Software Name | Purpose |
|---|---|
| Aimless | data scaling |
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| PHASER | phasing |
| XDS | data reduction |
Entry History & Funding Information
Deposition Data
- Released Date: 2018-02-28 Deposition Author(s): Jensen, M.R., Goblirsch, B.R., Esler, M.A., Christenson, J.K., Mohamed, F.A., Wackett, L.P., Wilmot, C.M.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | T32GM008700 |
| BioTechnology Institute | United States | 1000014885 10866 MNT11 |
Revision History (Full details and data files)
- Version 1.0: 2018-02-28
Type: Initial release - Version 1.1: 2020-01-01
Changes: Author supporting evidence - Version 1.2: 2023-10-04
Changes: Advisory, Data collection, Database references, Refinement description
