Research workbench
Crystal structure of A51V variant of human cytochrome C
Analyse Crystal structure of A51V variant of 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
- 6DUJ
- Type
- protein
- Length
- 208 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C
- UniProt
- P99999
- Ligands
- HEC
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Cytochrome C | protein | 104 | 41% helix, 2% strand | P99999 |
Ligands and binding sites
- HEC · Heme C · ligand · 2 copies · chains A, C
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 | 183 | 0.76 | 0.91 | 33 | HEC |
| 2 | 186 | 0.74 | 0.90 | 36 | HEC |
| 3 | 58 | 0.25 | 0.73 | 17 | empty |
| 4 | 59 | 0.24 | 0.72 | 15 | empty |
Interfaces
1 interface between chains.
- A–C · 511 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 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 6DUJ · PDBe 6DUJ · UniProt P99999
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