Research workbench
Crystal structure of dimeric K72A human cytochrome C alkaline conformer
Analyse Crystal structure of dimeric K72A human cytochrome C alkaline conformer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XNK
- 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
- 2 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G | Cytochrome C | protein | 104 | 51% helix, 2% strand | P99999 |
Ligands and binding sites
- HEC · Heme C · ligand · 4 copies · chains A, C, E, G
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 | 1012 | 0.85 | 0.85 | 92 | HEC |
| 2 | 1026 | 0.85 | 0.85 | 93 | HEC |
Interfaces
3 interfaces between chains.
- E–G · 2143 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 2094 Ų buried · 10 hydrogen bonds · protein-protein
- A–E · 99 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 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 6XNK · PDBe 6XNK · UniProt P99999
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