Download MendeleyCrystal structure of Methanothermobacter thermautotrophicus orotidine 5'-monophosphate decarboxylase covalently modified by 5-fluoro-6-iodo-UMP
Liu, Y., Kotra, L.P., Pai, E.F.To be published.
3SGU
Crystal structure of Methanothermobacter thermautotrophicus orotidine 5'-monophosphate decarboxylase covalently modified by 5-fluoro-6-iodo-UMP
- PDB DOI: https://doi.org/10.2210/pdb3SGU/pdb
- Classification: LYASE
- Organism(s): Methanothermobacter thermautotrophicus str. Delta H
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2011-06-15 Released: 2012-05-02
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.196
- R-Value Work: 0.164
- R-Value Observed: 0.166
Starting Model: experimental
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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 |
| Orotidine 5'-phosphate decarboxylase | 247 | Methanothermobacter thermautotrophicus str. Delta H | Mutation(s): 0 Gene Names: 1470090, MTH_129, pyrF EC: 4.1.1.23 |  | |
UniProt | |||||
Find proteins for O26232 (Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)) Explore O26232 Go to UniProtKB: O26232 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | O26232 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| 5FU Query on 5FU | B [auth A] | 5-FLUORO-URIDINE-5'-MONOPHOSPHATE C9 H12 F N2 O9 P RNBMPPYRHNWTMA-UAKXSSHOSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| CSD Query on CSD | A | L-PEPTIDE LINKING | C3 H7 N O4 S |  | CYS |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.196
- R-Value Work: 0.164
- R-Value Observed: 0.166
- Space Group: C 2 2 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 57.891 | α = 90 |
| b = 103.709 | β = 90 |
| c = 73.68 | γ = 90 |
| Software Name | Purpose |
|---|---|
| HKL-2000 | data collection |
| MOLREP | phasing |
| REFMAC | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
Entry History
Deposition Data
- Released Date: 2012-05-02 Deposition Author(s): Liu, Y., Kotra, L.P., Pai, E.F.
Revision History (Full details and data files)
- Version 1.0: 2012-05-02
Type: Initial release - Version 1.1: 2014-11-19
Changes: Structure summary - Version 1.2: 2023-09-13
Changes: Data collection, Database references, Derived calculations, Refinement description
