Research workbench
Molecular structure of cytochrome C2 isolated from rhodobacter capsulatus determined at 2.5 ångströms resolution
Analyse Molecular structure of cytochrome C2 isolated from rhodobacter capsulatus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1C2R
- Type
- protein
- Length
- 232 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C2
- UniProt
- P00094
- Ligands
- HEC
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cytochrome C2 | protein | 116 | 40% helix, 8% strand | P00094 |
Ligands and binding sites
- 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
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 217 | 0.74 | 0.89 | 36 | HEC |
| 2 | 227 | 0.73 | 0.87 | 37 | HEC |
| 3 | 159 | 0.56 | 0.81 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 346 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 cofactor (heme c attachment).
Compared structures
- 1C2R · Molecular structure of cytochrome C2 isolated from rhodobacter capsulatus determined at… · the same entry in another collection · chain A against A, TM-score 1.00
- P00094 · AlphaFold monomer V2.0 prediction for cytochrome C2 (P00094) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P00094
- Elsewhere: RCSB PDB 1C2R · PDBe 1C2R · UniProt P00094
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