Research workbench
Refined structure of cytochrome C3 at 1.8 ångströms resolution
Analyse Refined structure of cytochrome C3 at 1.8 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CDV
- Type
- protein
- Length
- 107 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C3
- UniProt
- P00132
- Ligands
- HEC
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C3 | protein | 107 | 28% helix, 11% strand | P00132 |
Ligands and binding sites
- HEC · Heme C · ligand · 4 copies · 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 | 665 | 0.75 | 0.81 | 68 | HEC |
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 P00132
- Elsewhere: RCSB PDB 2CDV · PDBe 2CDV · UniProt P00132
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