Research workbench
Structure of the allosteric regulatory enzyme of purine biosynthesis
Analyse Structure of the allosteric regulatory enzyme of purine biosynthesis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GPH
- Type
- protein
- Length
- 1,860 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00497
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1, 2, 3, 4 | — | protein | 465 | — | P00497 |
Compared structures
- 1GPH · Structure of the allosteric regulatory enzyme of purine biosynthesis · the same entry in another collection · chain 1 against 1, TM-score 1.00
- P00497 · AlphaFold monomer V2.0 prediction for amidophosphoribosyltransferase (P00497) · a predicted model of the same protein · chain 1 against A, TM-score 0.98
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 P00497
- Elsewhere: RCSB PDB 1GPH · PDBe 1GPH · UniProt P00497
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