Research workbench
Cyanuric acid hydrolase: evolutionary innovation by structural concatenation.
Analyse Cyanuric acid hydrolase: evolutionary innovation by structural concatenation. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BVS
- Type
- protein
- Length
- 728 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P58329
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 364 | — | P58329 |
Compared structures
- 4BVS · Cyanuric acid hydrolase: evolutionary innovation by structural concatenation. · the same entry in another collection · chain A against A, TM-score 1.00
- P58329 · AlphaFold monomer V2.0 prediction for cyanuric acid amidohydrolase (P58329) · a predicted model of the same protein · chain B 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 P58329
- Elsewhere: RCSB PDB 4BVS · PDBe 4BVS · UniProt P58329
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