Download MendeleyThe structure of a putative mannosephosphate isomerase from Archaeoglobus fulgidus
Cuff, M.E., Skarina, T., Edwards, A., Savchenko, A., Joachimiak, A.To be published.
1ZX5
The structure of a putative mannosephosphate isomerase from Archaeoglobus fulgidus
- PDB DOI: https://doi.org/10.2210/pdb1ZX5/pdb
- Classification: STRUCTURAL GENOMICS, UNKNOWN FUNCTION
- Organism(s): Archaeoglobus fulgidus
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2005-06-06 Released: 2005-07-19
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.30 Å
- R-Value Free: 0.191
- R-Value Work: 0.162
- R-Value Observed: 0.164
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 |
| mannosephosphate isomerase, putative | 300 | Archaeoglobus fulgidus | Mutation(s): 4 Gene Names: AF0035 EC: 5.3.1.8 |  | |
UniProt | |||||
Find proteins for O30200 (Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)) Explore O30200 Go to UniProtKB: O30200 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | O30200 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| LFR Query on LFR | B [auth A] | beta-L-fructofuranose C6 H12 O6 RFSUNEUAIZKAJO-AZGQCCRYSA-N |  | ||
| GOL Query on GOL | K [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| EDO Query on EDO | C [auth A], D [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| ACY Query on ACY | E [auth A] F [auth A] G [auth A] H [auth A] I [auth A] | ACETIC ACID C2 H4 O2 QTBSBXVTEAMEQO-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: 2.30 Å
- R-Value Free: 0.191
- R-Value Work: 0.162
- R-Value Observed: 0.164
- Space Group: P 43 3 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 160.045 | α = 90 |
| b = 160.045 | β = 90 |
| c = 160.045 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| SBC-Collect | data collection |
| HKL-2000 | data scaling |
| HKL-3000 | phasing |
| SHELXD | phasing |
| SHELXE | model building |
| MLPHARE | phasing |
| DM | phasing |
| SOLVE | phasing |
| RESOLVE | phasing |
| O | model building |
| Coot | model building |
| CCP4 | phasing |
| ARP/wARP | model building |
Entry History
Deposition Data
- Released Date: 2005-07-19 Deposition Author(s): Cuff, M.E., Skarina, T., Edwards, A., Savchenko, A., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2005-07-19
Type: Initial release - Version 1.1: 2008-04-30
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.3: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Data collection, Database references, Derived calculations, Structure summary - Version 1.4: 2024-11-06
Changes: Data collection, Database references, Structure summary
