Download MendeleyCrystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase from Aquifex aeolicus VF5
Kitamura, Y., Yokoyama, S., Kuramitsu, S.To be published.
2YVW | pdb_00002yvw
Crystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase from Aquifex aeolicus VF5
- PDB DOI: https://doi.org/10.2210/pdb2YVW/pdb
- Classification: TRANSFERASE
- Organism(s): Aquifex aeolicus VF5
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2007-04-16 Released: 2007-10-16
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.81 Å
- R-Value Free: 0.220 (Depositor), 0.210 (DCC)
- R-Value Work: 0.195 (Depositor), 0.190 (DCC)
- R-Value Observed: 0.195 (Depositor)
Starting Model: experimental
View more details
This is version 1.2 of the entry. See complete history.
Re-refinement Note
A newer entry is available that reflects an alternative modeling of the original data: 3SWG
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| UDP-N-acetylglucosamine 1-carboxyvinyltransferase | 425 | Aquifex aeolicus VF5 | Mutation(s): 0 EC: 2.5.1.7 |  | |
UniProt | |||||
Find proteins for O67315 (Aquifex aeolicus (strain VF5)) Explore O67315 Go to UniProtKB: O67315 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | O67315 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| EPU Query on EPU | C [auth A] | URIDINE-DIPHOSPHATE-2(N-ACETYLGLUCOSAMINYL) BUTYRIC ACID C20 H29 N3 O19 P2 BEGZZYPUNCJHKP-DBYWSUQTSA-N |  | ||
| PO4 Query on PO4 | B [auth A] | PHOSPHATE ION O4 P NBIIXXVUZAFLBC-UHFFFAOYSA-K |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.81 Å
- R-Value Free: 0.220 (Depositor), 0.210 (DCC)
- R-Value Work: 0.195 (Depositor), 0.190 (DCC)
- R-Value Observed: 0.195 (Depositor)
Space Group: P 62
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 132.004 | α = 90 |
| b = 132.004 | β = 90 |
| c = 58.165 | γ = 120 |
| Software Name | Purpose |
|---|---|
| CNS | refinement |
| HKL-2000 | data collection |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| PHENIX | phasing |
Entry History
Deposition Data
- Released Date: 2007-10-16 Deposition Author(s): Kitamuta, Y., Yokoyama, S., Kuramitsu, S., RIKEN Structural Genomics/Proteomics Initiative (RSGI)
Revision History (Full details and data files)
- Version 1.0: 2007-10-16
Type: Initial release - Version 1.1: 2011-07-13
Changes: Source and taxonomy, Version format compliance - Version 1.2: 2023-10-25
Changes: Data collection, Database references, Derived calculations, Refinement description
