Download MendeleyCrystal structure of human orotidine 5'-monophosphate decarboxylase complexed with 5-fluoro-UMP(produced from 5-fluoro-6-amino-UMP)
Liu, Y., Kotra, L.P., Pai, E.F.To be published.
3MW7
Crystal structure of human orotidine 5'-monophosphate decarboxylase complexed with 5-fluoro-UMP(produced from 5-fluoro-6-amino-UMP)
- PDB DOI: https://doi.org/10.2210/pdb3MW7/pdb
- Classification: LYASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2010-05-05 Released: 2011-04-06
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.32 ?
- R-Value Free: 0.265
- R-Value Work: 0.205
- R-Value Observed: 0.208
Starting Model: experimental
View more details
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 |
| Uridine 5'-monophosphate synthase | 312 | Homo sapiens | Mutation(s): 0 Gene Names: gi|13960142, OK/SW-cl.21, UMPS EC: 4.1.1.23 (PDB Primary Data), 2.4.2.10 (UniProt) |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P11172 (Homo sapiens) Explore P11172 Go to UniProtKB: P11172 | |||||
PHAROS: P11172 GTEx: ENSG00000114491 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P11172 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| 5FU Query on 5FU | C [auth A], D [auth B] | 5-FLUORO-URIDINE-5'-MONOPHOSPHATE C9 H12 F N2 O9 P RNBMPPYRHNWTMA-UAKXSSHOSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.32 ?
- R-Value Free: 0.265
- R-Value Work: 0.205
- R-Value Observed: 0.208
- Space Group: P 1 21 1
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 70.29 | ¦Á = 90 |
| b = 61.742 | ¦Â = 111.64 |
| c = 71.212 | ¦Ă = 90 |
| Software Name | Purpose |
|---|---|
| HKL-2000 | data collection |
| MOLREP | phasing |
| REFMAC | refinement |
| Coot | model building |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
Entry History
Deposition Data
- Released Date: 2011-04-06 Deposition Author(s): Liu, Y., Kotra, L.P., Pai, E.F.
Revision History (Full details and data files)
- Version 1.0: 2011-04-06
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2023-09-06
Changes: Data collection, Database references, Derived calculations, Refinement description
