MolNFT v1 · #17554 · protein
Towards understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerophosphate synthase
1OX4: “Towards understanding the mechanism of the complex cyclization reaction catalyzed by imidazole…”. X-ray diffraction. MolNFT v1 #17554 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1OX4
- Type
- protein
- Length
- 1,072 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P33734
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 534 | — | P33734 |
| B | — | protein | 538 | — | P33734 |
Compared structures
- 1OX4 · Towards understanding the mechanism of the complex cyclization reaction catalyzed by… · the same entry in another collection · chain A against A, TM-score 1.00
- P33734 · AlphaFold monomer V2.0 prediction for imidazole glycerol phosphate synthase hishf (P33734) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P33734
- Elsewhere: RCSB PDB 1OX4 · PDBe 1OX4 · UniProt P33734
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