MolNFT v1 · #16813 · protein
Reduced hybrid cluster protein (hcp) from desulfovibrio vulgaris hildenborough structure at 1.55A resolution using synchrotron radiation.
1OA1 · Hydroxylamine reductase: “Reduced hybrid cluster protein (hcp) from desulfovibrio vulgaris hildenborough structure at 1.55A resolution…”. X-ray diffraction, 2 ligands (SF4, SF3), 5 pockets (best druggability 0.69). MolNFT v1 #16813…
- PDB
- 1OA1
- Type
- protein
- Length
- 553 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hydroxylamine reductase
- EC
- 1.7.-.-
- UniProt
- P31101
- Ligands
- SF4, SF3
- Pockets
- 5 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydroxylamine reductase (EC 1.7.-.-) | protein | 553 | 51% helix, 11% strand | P31101 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · chains A
- SF3 · FE4-S3 cluster · ligand · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.69 | 0.97 | 18 | empty |
| 2 | 51 | 0.58 | 0.90 | 18 | empty |
| 3 | 158 | 0.53 | 0.80 | 28 | empty |
| 4 | 88 | 0.43 | 0.79 | 16 | empty |
| 5 | 91 | 0.40 | 0.78 | 15 | empty |
Compared structures
- 1OA1 · Reduced hybrid cluster protein (hcp) from desulfovibrio vulgaris hildenborough structure… · the same entry in another collection · chain A against A, TM-score 1.00
- P31101 · AlphaFold monomer V2.0 prediction for hydroxylamine reductase (P31101) · a predicted model of the same protein · 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 P31101
- Elsewhere: RCSB PDB 1OA1 · PDBe 1OA1 · UniProt P31101
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