MolNFT v1 · #113859 · protein
Hydrogenobacter thermophilus cytochrome C552 dimer formed by domain swapping at C-terminal region
5AUS · Cytochrome C-552: “Hydrogenobacter thermophilus cytochrome C552 dimer formed by domain swapping at C-terminal region”. X-ray diffraction, 1 ligand (HEC), 2 pockets (best druggability 0.75). MolNFT v1 #113859 on GenesisL1: 3D…
- PDB
- 5AUS
- Type
- protein
- Length
- 162 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C-552
- UniProt
- P15452
- Ligands
- HEC
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C-552 | protein | 79 | 51% helix, 3% strand | P15452 |
| C | Cytochrome C-552 | protein | 83 | 48% helix, 2% strand | P15452 |
Ligands and binding sites
- HEC · Heme C · ligand · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 287 | 0.75 | 0.88 | 45 | HEC |
| 2 | 312 | 0.73 | 0.86 | 46 | HEC |
Interfaces
1 interface between chains.
- A–C · 2375 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 cofactor (heme c attachment).
Compared structures
- 5AUS · Hydrogenobacter thermophilus cytochrome c552 dimer formed by domain swapping at… · the same entry in another collection · chain C against C, TM-score 1.00
- P15452 · AlphaFold monomer V2.0 prediction for cytochrome C-552 (P15452) · a predicted model of the same protein · chain A against A, TM-score 0.66
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 P15452
- Elsewhere: RCSB PDB 5AUS · PDBe 5AUS · UniProt P15452
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