Research workbench
Cytochrome C at low ionic strength
Analyse Cytochrome C at low ionic strength in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CRC
- Type
- protein
- Length
- 208 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C
- UniProt
- P00004
- Ligands
- ACE, HEC
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cytochrome C | protein | 104 | 41% helix, 2% strand | P00004 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 196 | 0.77 | 0.92 | 35 | HEC |
| 2 | 223 | 0.75 | 0.89 | 35 | HEC |
| 3 | 60 | 0.28 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 134 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 P00004
- Elsewhere: RCSB PDB 1CRC · PDBe 1CRC · UniProt P00004
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