Download MendeleyInosine 5'-monophosphate dehydrogenase from Vibrio cholerae complexed with IMP and mycophenolic acid.
Osipiuk, J., Maltseva, N., Makowska-Grzyska, M., Jedrzejczak, R., Anderson, W.F., Joachimiak, A.To be published.
4FXS | pdb_00004fxs
Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae complexed with IMP and mycophenolic acid
- PDB DOI: https://doi.org/10.2210/pdb4FXS/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Vibrio cholerae O1 biovar El Tor str. N16961
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2012-07-03 Released: 2012-07-25
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.24 Å
- R-Value Free: 0.232 (Depositor), 0.232 (DCC)
- R-Value Work: 0.190 (Depositor), 0.189 (DCC)
- R-Value Observed: 0.192 (Depositor)
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 |
| Inosine-5'-monophosphate dehydrogenase | 496 | Vibrio cholerae O1 biovar El Tor str. N16961 | Mutation(s): 0 Gene Names: VC0767, VC_0767 EC: 1.1.1.205 |  | |
UniProt | |||||
Find proteins for Q9KTW3 (Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)) Explore Q9KTW3 Go to UniProtKB: Q9KTW3 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9KTW3 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| IMP Query on IMP | B [auth A] | INOSINIC ACID C10 H13 N4 O8 P GRSZFWQUAKGDAV-KQYNXXCUSA-N |  | ||
| MOA Query on MOA | C [auth A] | MYCOPHENOLIC ACID C17 H20 O6 HPNSFSBZBAHARI-RUDMXATFSA-N |  | ||
| K Query on K | D [auth A] | POTASSIUM ION K NPYPAHLBTDXSSS-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: 2.24 Å
- R-Value Free: 0.232 (Depositor), 0.232 (DCC)
- R-Value Work: 0.190 (Depositor), 0.189 (DCC)
- R-Value Observed: 0.192 (Depositor)
Diffraction Data: https://doi.org/10.18430/m34fxs
Space Group: I 4 2 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 111.96 | α = 90 |
| b = 111.96 | β = 90 |
| c = 188.994 | γ = 90 |
| Software Name | Purpose |
|---|---|
| DENZO | data reduction |
| SCALEPACK | data scaling |
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| SBC-Collect | data collection |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| PHENIX | phasing |
Entry History
Deposition Data
- Released Date: 2012-07-25 Deposition Author(s): Osipiuk, J., Maltseva, N., Makowska-Grzyska, M., Jedrzejczak, R., Anderson, W.F., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)
Revision History (Full details and data files)
- Version 1.0: 2012-07-25
Type: Initial release - Version 1.1: 2017-11-15
Changes: Refinement description - Version 1.2: 2024-10-30
Changes: Data collection, Database references, Derived calculations, Structure summary
