Research workbench
Arsenate reductase (arsc from PI258) C10S/C15A double mutant with sulfate in its active site
Analyse Arsenate reductase (arsc from PI258) C10S/C15A double mutant with sulfate in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FXI
- Type
- protein
- Length
- 131 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein arsc
- EC
- 1.20.4.-, 3.1.3.48
- UniProt
- P0A006
- Ligands
- K, SO4
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein arsc (EC 1.20.4.-, 3.1.3.48) | protein | 131 | 39% helix, 18% strand | P0A006 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2FXI · Arsenate reductase (ArsC from pI258) C10S/C15A double mutant with sulfate in its active… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A006 · AlphaFold monomer V2.0 prediction for arsenate reductase (P0A006) · a predicted model of the same protein · chain A 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 P0A006
- Elsewhere: RCSB PDB 2FXI · PDBe 2FXI · UniProt P0A006
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