MolNFT v1 · #74381 · protein
Structure of dodecaheme cytochrome C GSU1996
3OV0 · Cytochrome C family protein: “Structure of dodecaheme cytochrome C GSU1996”. X-ray diffraction, 1 ligand (HEC), 2 pockets (best druggability 0.82). MolNFT v1 #74381 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3OV0
- Type
- protein
- Length
- 318 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C family protein
- UniProt
- Q74BP5
- Ligands
- HEC
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C family protein | protein | 318 | 20% helix, 13% strand | Q74BP5 |
Ligands and binding sites
- HEC · Heme C · ligand · 12 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 978 | 0.82 | 0.83 | 121 | HEC |
| 2 | 992 | 0.81 | 0.82 | 107 | HEC |
Modifications
Observed in the structure: 24 cofactor (heme c attachment).
Compared structures
- 3OV0 · Structure of dodecaheme cytochrome c GSU1996 · 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 Q74BP5
- Elsewhere: RCSB PDB 3OV0 · PDBe 3OV0 · UniProt Q74BP5
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