Research workbench
Mutant M58H of nostoc sp cytochrome C6
Analyse Mutant M58H of nostoc sp cytochrome C6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4H0K
- Type
- protein
- Length
- 171 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C6
- UniProt
- P0A3X7
- Ligands
- HEC
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C6 | protein | 86 | 58% helix, 0% strand | P0A3X7 |
| B | Cytochrome C6 | protein | 85 | 56% helix, 2% strand | P0A3X7 |
Ligands and binding sites
- HEC · Heme C · ligand · 2 copies · chains A, B
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 | 328 | 0.75 | 0.86 | 45 | HEC |
| 2 | 176 | 0.65 | 0.85 | 29 | HEC |
Interfaces
1 interface between chains.
- A–B · 492 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 cofactor (heme c 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 P0A3X7
- Elsewhere: RCSB PDB 4H0K · PDBe 4H0K · UniProt P0A3X7
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