Research workbench
Crystal structure of cytochrome C6C from synechococcus sp. pcc 7002
Analyse Crystal structure of cytochrome C6C 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
- 4EIE
- 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 0.68
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 · 4 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 | 229 | 0.68 | 0.84 | 30 | HEC |
Modifications
Observed in the structure: 2 cofactor (heme c attachment).
Compared structures
- 4EIE · Crystal structure of cytochrome c6C 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 4EIE · PDBe 4EIE · UniProt Q8KX15
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