MolNFT v1 · #13666 · protein
Wild type PI258 S. aureus arsenate reductase
1LJL: “Wild type PI258 S. aureus arsenate reductase”. X-ray diffraction, 1 ligand (K). MolNFT v1 #13666 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1LJL
- Type
- protein
- Length
- 130 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arsenate reductase
- EC
- 1.97.1.5
- UniProt
- P0A006
- Ligands
- K
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arsenate reductase (EC 1.97.1.5) | protein | 130 | 38% helix, 17% strand | P0A006 |
Ligands and binding sites
- K · Potassium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 1LJL · PDBe 1LJL · UniProt P0A006
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