Download MendeleyHuman UMP Synthase (C-terminal Domain-Orotidine 5'-Monophosphate Decarboxylase)
Liu, Y., Tang, H.L., Pai, E.F.To be published.
2P1F
Human UMP Synthase (C-terminal Domain-Orotidine 5'-Monophosphate Decarboxylase)
- PDB DOI: https://doi.org/10.2210/pdb2P1F/pdb
- Classification: HYDROLASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2007-03-05 Released: 2007-04-03
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.76 ?
- R-Value Free: 0.171
- R-Value Work: 0.139
- R-Value Observed: 0.141
Starting Model: experimental
View more details
wwPDB Validation 3D Report Full Report
This is version 1.3 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 | 291 | Homo sapiens | Mutation(s): 1 Gene Names: UMPS EC: 2.4.2.10 (UniProt), 4.1.1.23 (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 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| SO4 Query on SO4 | B [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| GOL Query on GOL | D [auth A], E [auth A], F [auth A], G [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| NA Query on NA | C [auth A] | SODIUM ION Na FKNQFGJONOIPTF-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| CSX Query on CSX | A | L-PEPTIDE LINKING | C3 H7 N O3 S |  | CYS |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.76 ?
- R-Value Free: 0.171
- R-Value Work: 0.139
- R-Value Observed: 0.141
- Space Group: C 2 2 21
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 78.314 | ¦Á = 90 |
| b = 116.875 | ¦Â = 90 |
| c = 61.946 | ¦Ă = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| ADSC | data collection |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| MOLREP | phasing |
Entry History
Deposition Data
- Released Date: 2007-04-03 Deposition Author(s): Liu, Y., Tang, H.L., Pai, E.F.
Revision History (Full details and data files)
- Version 1.0: 2007-04-03
Type: Initial release - Version 1.1: 2008-05-01
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Derived calculations, Version format compliance - Version 1.3: 2023-08-30
Changes: Data collection, Database references, Derived calculations, Refinement description
