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Crystal structure of human orotidine 5'-monophosphate decarboxylase covalently modified by 5-fluoro-6-azido-ump
Analyse Crystal structure of human orotidine 5'-monophosphate decarboxylase covalently… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3G3D
- Type
- protein
- Length
- 515 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P11172
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 256 | — | P11172 |
| B | — | protein | 259 | — | P11172 |
Compared structures
- 3G3D · Crystal Structure of Human Orotidine 5'-monophosphate Decarboxylase Covalently Modified… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P11172
- Elsewhere: RCSB PDB 3G3D · PDBe 3G3D · UniProt P11172
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