Research workbench
Structure of recombinant human cytochrome C
Analyse Structure of recombinant human cytochrome C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZCF
- Type
- protein
- Length
- 416 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C
- UniProt
- P99999
- Ligands
- HEC
- Pockets
- 5 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Cytochrome C | protein | 104 | 41% helix, 2% strand | P99999 |
Ligands and binding sites
- HEC · Heme C · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 270 | 0.81 | 0.92 | 44 | HEC |
| 2 | 286 | 0.79 | 0.90 | 46 | HEC |
| 3 | 184 | 0.75 | 0.90 | 34 | HEC |
| 4 | 294 | 0.73 | 0.86 | 45 | HEC |
| 5 | 428 | 0.58 | 0.74 | 41 | empty |
Interfaces
4 interfaces between chains.
- A–B · 429 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 397 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 277 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 56 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 5 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 P99999
- Elsewhere: RCSB PDB 3ZCF · PDBe 3ZCF · UniProt P99999
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