Research workbench
Crystal structure of the reduced form of cytochrome C" from methylophilus methylotrophus
Analyse Crystal structure of the reduced form of cytochrome C" from methylophilus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OAE
- Type
- protein
- Length
- 248 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C"
- UniProt
- Q9RQB9
- Ligands
- HEC, SO4
- Pockets
- 1 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cytochrome C" | protein | 124 | 48% helix, 6% strand | Q9RQB9 |
Ligands and binding sites
- HEC · Heme C · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 6 copies · chains A, B
- GOL · Glycerol · additive · 5 copies · chains A, B
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 | 967 | 0.82 | 0.83 | 93 | HEC, GOL, SO4 |
Interfaces
1 interface between chains.
- A–B · 650 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 cofactor (heme c attachment).
Compared structures
- 1OAE · Crystal structure of the reduced form of cytochrome c" from Methylophilus methylotrophus · the same entry in another collection · chain A against A, TM-score 1.00
- Q9RQB9 · AlphaFold monomer V2.0 prediction for cytochrome C'' (Q9RQB9) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 Q9RQB9
- Elsewhere: RCSB PDB 1OAE · PDBe 1OAE · UniProt Q9RQB9
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