MolNFT v1 · #4709 · protein
Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site
1DW9: “Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for…”. X-ray diffraction. MolNFT v1 #4709 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1DW9
- Type
- protein
- Length
- 1,560 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00816
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | — | protein | 156 | — | P00816 |
Compared structures
- 1DW9 · Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits… · the same entry in another collection · chain J against J, TM-score 1.00
- P00816 · AlphaFold monomer V2.0 prediction for cyanate hydratase (P00816) · a predicted model of the same protein · chain F 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 P00816
- Elsewhere: RCSB PDB 1DW9 · PDBe 1DW9 · UniProt P00816
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.