MolNFT v1 · #183912 · protein
Structure of cyanase from pseudomonas lactis
7O74 · Cyanate hydratase: “Structure of cyanase from pseudomonas lactis”. X-ray diffraction, 1 ligand (CL), 20 pockets (best druggability 0.78). MolNFT v1 #183912 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7O74
- Type
- protein
- Length
- 1,560 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyanate hydratase
- EC
- 4.2.1.104
- UniProt
- A0A218ZZ45
- Ligands
- CL
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | Cyanate hydratase (EC 4.2.1.104) | protein | 156 | 46% helix, 20% strand | A0A218ZZ45 |
Ligands and binding sites
- CL · Chloride ion · ion · 9 copies · chains A, D, I, J, B, F, C, H, E, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.78 | 0.99 | 18 | empty |
| 2 | 75 | 0.76 | 0.98 | 19 | empty |
| 3 | 72 | 0.76 | 0.98 | 18 | empty |
| 4 | 71 | 0.75 | 0.98 | 18 | empty |
| 5 | 68 | 0.75 | 0.98 | 18 | empty |
Interfaces
25 interfaces between chains.
- A–D · 3377 Ų buried · 55 hydrogen bonds · protein-protein
- E–G · 3371 Ų buried · 55 hydrogen bonds · protein-protein
- B–F · 3366 Ų buried · 56 hydrogen bonds · protein-protein
- I–J · 3361 Ų buried · 55 hydrogen bonds · protein-protein
- C–H · 3356 Ų buried · 55 hydrogen bonds · protein-protein
Compared structures
- 7O74 · Structure of cyanase from Pseudomonas lactis · the same entry in another collection · chain E against E, 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 A0A218ZZ45
- Elsewhere: RCSB PDB 7O74 · PDBe 7O74 · UniProt A0A218ZZ45
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