Download MendeleyCrystal structure of GMP synthetase from Thermus thermophilus
Baba, S., Kanagawa, M., Yanai, H., Ishii, T., Kuramitsu, S., Yokoyama, S., Sampei, G., Kawai, G.To be published.
2YWC
Crystal structure of GMP synthetase from Thermus thermophilus in complex with XMP
- PDB DOI: https://doi.org/10.2210/pdb2YWC/pdb
- Classification: LIGASE
- Organism(s): Thermus thermophilus HB8
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2007-04-20 Released: 2007-10-23
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 ?
- R-Value Free: 0.278
- R-Value Work: 0.236
- R-Value Observed: 0.236
Starting Model: experimental
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This is version 1.4 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 |
| GMP synthase [glutamine-hydrolyzing] | 503 | Thermus thermophilus HB8 | Mutation(s): 0 Gene Names: guaA EC: 6.3.5.2 |  | |
UniProt | |||||
Find proteins for Q5SI28 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)) Explore Q5SI28 Go to UniProtKB: Q5SI28 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q5SI28 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| XMP Query on XMP | E [auth A], F [auth B], G [auth C], H [auth D] | XANTHOSINE-5'-MONOPHOSPHATE C10 H14 N4 O9 P DCTLYFZHFGENCW-UUOKFMHZSA-O |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B, C, D | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 ?
- R-Value Free: 0.278
- R-Value Work: 0.236
- R-Value Observed: 0.236
- Space Group: C 1 2 1
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 142.58 | ¦Á = 90 |
| b = 115.213 | ¦Â = 93.21 |
| c = 159.348 | ¦Ă = 90 |
| Software Name | Purpose |
|---|---|
| CNS | refinement |
| HKL-2000 | data collection |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| MOLREP | phasing |
Entry History
Deposition Data
- Released Date: 2007-10-23 Deposition Author(s): Baba, S., Kanagawa, M., Kuramitsu, S., Yokoyama, S., Sampei, G., Kawai, G., RIKEN Structural Genomics/Proteomics Initiative (RSGI)
Revision History (Full details and data files)
- Version 1.0: 2007-10-23
Type: Initial release - Version 1.1: 2011-07-13
Changes: Derived calculations, Source and taxonomy, Version format compliance - Version 1.2: 2023-10-25
Changes: Data collection, Database references, Derived calculations, Refinement description - Version 1.3: 2023-11-15
Changes: Data collection - Version 1.4: 2024-10-23
Changes: Structure summary
