MolNFT v1 · #16812 · protein
Reduced hybrid cluster protein from desulfovibrio desulfuricans X-ray structure at 1.25A resolution
1OA0 · Prismane protein: “Reduced hybrid cluster protein from desulfovibrio desulfuricans X-ray structure at 1.25A resolution”. X-ray diffraction, 2 ligands (SF4, SF3), 12 pockets (best druggability 0.77). MolNFT v1 #16812 on GenesisL1: 3D…
- PDB
- 1OA0
- Type
- protein
- Length
- 1,086 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prismane protein
- UniProt
- Q01770
- Ligands
- SF4, SF3
- Pockets
- 12 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Prismane protein | protein | 543 | 51% helix, 11% strand | Q01770 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · 2 copies · chains A, B
- SF3 · FE4-S3 cluster · ligand · 2 copies · chains A, B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 152 | 0.77 | 0.94 | 57 | empty |
| 2 | 61 | 0.67 | 0.94 | 27 | empty |
| 3 | 73 | 0.63 | 0.90 | 24 | empty |
| 4 | 56 | 0.61 | 0.91 | 22 | empty |
| 5 | 114 | 0.48 | 0.80 | 19 | empty |
Compared structures
- 1OA0 · Reduced hybrid cluster protein from desulfovibrio desulfuricans X-ray structure at 1.25A… · the same entry in another collection · chain A against A, TM-score 1.00
- Q01770 · AlphaFold monomer V2.0 prediction for hydroxylamine reductase (Q01770) · 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 Q01770
- Elsewhere: RCSB PDB 1OA0 · PDBe 1OA0 · UniProt Q01770
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