Research workbench
Redox conformation changes in refined tuna cytochrome C
Analyse Redox conformation changes in refined tuna cytochrome C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CYT
- Type
- protein
- Length
- 206 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C
- UniProt
- P81459
- Ligands
- ACE, HEC
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| O, I | Cytochrome C | protein | 103 | 42% helix, 2% strand | P81459 |
Ligands and binding sites
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 | 192 | 0.78 | 0.92 | 34 | HEC |
| 2 | 182 | 0.76 | 0.91 | 34 | HEC |
| 3 | 64 | 0.37 | 0.78 | 16 | empty |
| 4 | 55 | 0.31 | 0.76 | 12 | empty |
Interfaces
1 interface between chains.
- O–I · 253 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 cofactor, 2 covalent (heme c attachment, covalent ligand).
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 P81459
- Elsewhere: RCSB PDB 3CYT · PDBe 3CYT · UniProt P81459
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