Research workbench
Cocrystal of cytochrome C and sulfonato-THIACALIX[4]ARENE
Analyse Cocrystal of cytochrome C and sulfonato-THIACALIX[4]ARENE in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PR2
- Type
- protein
- Length
- 216 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C iso-1
- UniProt
- P00044
- Ligands
- 80M, HEC
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cytochrome C iso-1 | protein | 108 | 42% helix, 2% strand | P00044 |
Ligands and binding sites
- 80M · sulfonato-thiacalix[4]arene · ligand · 3 copies · chains A, B
- HEC · Heme C · 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 | 198 | 0.79 | 0.93 | 32 | HEC |
| 2 | 195 | 0.76 | 0.91 | 34 | HEC |
| 3 | 193 | 0.50 | 0.77 | 19 | empty |
| 4 | 172 | 0.49 | 0.77 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 445 Ų buried · 11 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 P00044
- Elsewhere: RCSB PDB 7PR2 · PDBe 7PR2 · UniProt P00044
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