Research workbench
Recombinantly produced KUSTA0087/KUSTA0088 complex, C32G/WT mutant
Analyse Recombinantly produced KUSTA0087/KUSTA0088 complex, C32G/WT mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6R6O
- Type
- protein
- Length
- 211 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Small soluble cyt C; KUSTA0088
- UniProt
- Q1Q7P4, Q1Q7P3
- Ligands
- HEC, K
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 64% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Small soluble cyt C | protein | 111 | 78% helix, 0% strand | Q1Q7P4 |
| B | KUSTA0088 | protein | 100 | 49% helix, 4% strand | Q1Q7P3 |
Ligands and binding sites
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 | 226 | 0.66 | 0.84 | 26 | HEC |
| 2 | 163 | 0.66 | 0.86 | 27 | HEC |
Interfaces
1 interface between chains.
- A–B · 1036 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 cofactor (heme c attachment).
Compared structures
- 6R6O · Recombinantly produced Kusta0087/Kusta0088 Complex, C32G/wt mutant · the same entry in another collection · chain A against A, TM-score 1.00
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 Q1Q7P4
- Every structure of UniProt Q1Q7P3
- Elsewhere: RCSB PDB 6R6O · PDBe 6R6O · UniProt Q1Q7P4 · UniProt Q1Q7P3
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