Research workbench
The cytochrome C552/CUA complex from thermus thermophilus
Analyse The cytochrome C552/CUA complex from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FWL
- Type
- protein
- Length
- 263 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C-552; Cytochrome C oxidase subunit II
- EC
- 1.9.3.1
- UniProt
- P04164, P98052
- Ligands
- HEC, CUA
- Pockets
- 1 · best druggability 0.76
Structure
solution nmr · 2 distinct chains · 26% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C-552 | protein | 129 | 45% helix, 6% strand | P04164 |
| B | Cytochrome C oxidase subunit II (EC 1.9.3.1) | protein | 134 | 8% helix, 45% strand | P98052 |
Ligands and binding sites
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 | 422 | 0.76 | 0.85 | 71 | HEC |
Interfaces
1 interface between chains.
- A–B · 641 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (heme c attachment).
Compared structures
- 2FWL · The cytochrome c552/CuA complex from Thermus thermophilus · the same entry in another collection · chain A against A, TM-score 1.00
- P04164 · AlphaFold monomer V2.0 prediction for cytochrome C-552 (P04164) · a predicted model of the same protein · chain A against A, TM-score 0.96
- P98052 · AlphaFold monomer V2.0 prediction for cytochrome C oxidase subunit 2 (P98052) · a predicted model of the same protein · chain B against A, TM-score 0.92
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 P04164
- Every structure of UniProt P98052
- Elsewhere: RCSB PDB 2FWL · PDBe 2FWL · UniProt P04164 · UniProt P98052
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