Research workbench
Cytochrome C' from rhodopseudomonas palustris
Analyse Cytochrome C' from rhodopseudomonas palustris in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1A7V
- Type
- protein
- Length
- 250 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C'
- UniProt
- P00149
- Ligands
- HEM
- Pockets
- 4 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 75% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cytochrome C' | protein | 125 | 75% helix, 2% strand | P00149 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
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 | 205 | 0.66 | 0.84 | 28 | HEM |
| 2 | 179 | 0.61 | 0.82 | 26 | HEM |
| 3 | 96 | 0.50 | 0.82 | 20 | empty |
| 4 | 146 | 0.47 | 0.77 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 560 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 cofactor (heme 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 P00149
- Elsewhere: RCSB PDB 1A7V · PDBe 1A7V · UniProt P00149
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