MolNFT v1 · #13679 · protein
Disulfide intermediate of C89L arsenate reductase from PI258
1LK0: “Disulfide intermediate of C89L arsenate reductase from PI258”. X-ray diffraction, 2 ligands (K, CL), 1 pocket (best druggability 0.64). MolNFT v1 #13679 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1LK0
- Type
- protein
- Length
- 260 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arsenate reductase
- EC
- 1.97.1.5
- UniProt
- P0A006
- Ligands
- K, CL
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Arsenate reductase (EC 1.97.1.5) | protein | 130 | 37% helix, 18% strand | P0A006 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 333 | 0.64 | 0.80 | 48 | CL |
Interfaces
1 interface between chains.
- A–B · 440 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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 P0A006
- Elsewhere: RCSB PDB 1LK0 · PDBe 1LK0 · UniProt P0A006
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