Research workbench
Reduced hybrid cluster protein (hcp) from desulfovibrio vulgaris hildenborough structure at 1.55A resolution using synchrotron radiation.
Analyse Reduced hybrid cluster protein (hcp) from desulfovibrio vulgaris hildenborough… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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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