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Crystal structure of arsenate reductase from archaeoglobus fulgidus dsm 4304, structural genomics
Analyse Crystal structure of arsenate reductase from archaeoglobus fulgidus dsm 4304… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Y1L
- Type
- protein
- Length
- 496 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arsenate reductase (arsc)
- UniProt
- O28910
- Ligands
- CD
- Pockets
- 9 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Arsenate reductase (arsc) | protein | 124 | 32% helix, 18% strand | O28910 |
Ligands and binding sites
- CD · Cadmium ion · metal · 8 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 522 | 0.71 | 0.80 | 65 | CD |
| 2 | 407 | 0.68 | 0.80 | 37 | empty |
| 3 | 401 | 0.67 | 0.80 | 33 | empty |
| 4 | 251 | 0.51 | 0.75 | 29 | empty |
| 5 | 235 | 0.50 | 0.75 | 28 | empty |
Interfaces
4 interfaces between chains.
- B–C · 766 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 764 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 566 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 564 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1Y1L · Crystal structure of arsenate reductase from Archaeoglobus fulgidus DSM 4304, structural… · the same entry in another collection · chain A 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 O28910
- Elsewhere: RCSB PDB 1Y1L · PDBe 1Y1L · UniProt O28910
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