Download MendeleyX-ray Crystal Structure of Serine Hydroxymethyl Transferase from Burkholderia cenocepacia bound to PLP and Serine
Fairman, J.W., Jensen, M.M., Sullivan, A.H., Edwards, T.E., Lorimer, D.To be published.
4OT8
X-ray Crystal Structure of Serine Hydroxymethyl Transferase from Burkholderia cenocepacia bound to PLP and Serine
- PDB DOI: https://doi.org/10.2210/pdb4OT8/pdb
- Classification: TRANSFERASE
- Organism(s): Burkholderia cenocepacia J2315
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2014-02-13 Released: 2014-04-23
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.00 Å
- R-Value Free: 0.206 (Depositor), 0.210 (DCC)
- R-Value Work: 0.165 (Depositor), 0.180 (DCC)
- R-Value Observed: 0.168 (Depositor)
Starting Model: experimental
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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 |
| Serine hydroxymethyltransferase | 423 | Burkholderia cenocepacia J2315 | Mutation(s): 0 Gene Names: glyA, BCAL3197 EC: 2.1.2.1 |  | |
UniProt | |||||
Find proteins for B4ECY9 (Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)) Explore B4ECY9 Go to UniProtKB: B4ECY9 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | B4ECY9 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PLP Query on PLP | E [auth A], H [auth B], K [auth C], L [auth D] | PYRIDOXAL-5'-PHOSPHATE C8 H10 N O6 P NGVDGCNFYWLIFO-UHFFFAOYSA-N |  | ||
| SER Query on SER | F [auth A], G [auth A], I [auth B], J [auth B] | SERINE C3 H7 N O3 MTCFGRXMJLQNBG-REOHCLBHSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.00 Å
- R-Value Free: 0.206 (Depositor), 0.210 (DCC)
- R-Value Work: 0.165 (Depositor), 0.180 (DCC)
- R-Value Observed: 0.168 (Depositor)
Diffraction Data: https://doi.org/10.18430/M34OT8
Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 66.22 | α = 90 |
| b = 179.84 | β = 115.25 |
| c = 75.64 | γ = 90 |
| Software Name | Purpose |
|---|---|
| XSCALE | data scaling |
| PHASER | phasing |
| PHENIX | refinement |
| PDB_EXTRACT | data extraction |
Entry History
Deposition Data
- Released Date: 2014-04-23 Deposition Author(s): Seattle Structural Genomics Center for Infectious Disease (SSGCID)
Revision History (Full details and data files)
- Version 1.0: 2014-04-23
Type: Initial release - Version 1.1: 2023-09-20
Changes: Data collection, Database references, Derived calculations, Refinement description
