MolNFT v1 · #20370 · protein
Cytochrome C'
1RCP: “Cytochrome C'”. X-ray diffraction, 1 ligand (HEM), 4 pockets (best druggability 0.68). MolNFT v1 #20370 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1RCP
- Type
- protein
- Length
- 258 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C'
- UniProt
- P00147
- Ligands
- HEM
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cytochrome C' | protein | 129 | 74% helix, 2% strand | P00147 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.68 | 0.84 | 30 | HEM |
| 2 | 271 | 0.67 | 0.83 | 38 | HEM |
| 3 | 73 | 0.29 | 0.73 | 16 | empty |
| 4 | 70 | 0.29 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 565 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 cofactor (heme 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 P00147
- Elsewhere: RCSB PDB 1RCP · PDBe 1RCP · UniProt P00147
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