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Crystal structure of ferricytochrome C2 from rhodopseudomonas viridis
Analyse Crystal structure of ferricytochrome C2 from rhodopseudomonas viridis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IO3
- Type
- protein
- Length
- 107 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.9
- Source
- Blastochloris viridis
- Molecule
- Cytochrome C2
- UniProt
- P00083
- Ligands
- HEC
- Pockets
- 1 · best druggability 0.72
Structure
x-ray diffraction · resolution 1.9 · 1 distinct chain · 37% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C2 | protein | 107 | 37% helix, 4% strand | P00083 |
Ligands and binding sites
- HEC · Heme C · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 190 | 0.72 | 0.88 | 31 | HEC |
Modifications
Observed in the structure: 2 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 P00083
- Elsewhere: RCSB PDB 1IO3 · PDBe 1IO3 · UniProt P00083
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