Research workbench
Crystal structure of cytochrome C6C L50Q mutant from synechococcus sp. pcc 7002
Analyse Crystal structure of cytochrome C6C L50Q mutant from synechococcus sp. pcc 7002 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EIF
- Type
- protein
- Length
- 82 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C6
- UniProt
- Q8KX15
- Ligands
- HEC, NA, CL
- Pockets
- 1 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C6 | protein | 82 | 60% helix, 2% strand | Q8KX15 |
Ligands and binding sites
- HEC · Heme C · ligand · chains A
- NA · Sodium ion · metal · 3 copies · chains A
- CL · Chloride ion · ion · 4 copies · chains A
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 | 203 | 0.69 | 0.86 | 31 | HEC, CL |
Modifications
Observed in the structure: 2 cofactor (heme c attachment).
Compared structures
- 4EIF · Crystal structure of cytochrome c6C L50Q mutant from Synechococcus sp. PCC 7002 · 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 Q8KX15
- Elsewhere: RCSB PDB 4EIF · PDBe 4EIF · UniProt Q8KX15
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