MolNFT v1 · #148725 · protein
X-ray structure of bovine heart cytochrome C at high ionic strength
6FF5: “X-ray structure of bovine heart cytochrome C at high ionic strength”. X-ray diffraction, 3 ligands (HEC, NO3, SO4), 1 pocket (best druggability 0.75). MolNFT v1 #148725 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6FF5
- Type
- protein
- Length
- 104 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C
- UniProt
- P62894
- Ligands
- HEC, NO3, SO4
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C | protein | 104 | 41% helix, 2% strand | P62894 |
Ligands and binding sites
- HEC · Heme C · ligand · chains A
- NO3 · Nitrate ion · ion · 5 copies · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 211 | 0.75 | 0.90 | 36 | HEC |
Modifications
Observed in the structure: 2 cofactor (heme c attachment).
Compared structures
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 P62894
- Elsewhere: RCSB PDB 6FF5 · PDBe 6FF5 · UniProt P62894
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