Research workbench
Reduced state of cytochrome C554 from nitrosomonas europaea
Analyse Reduced state of cytochrome C554 from nitrosomonas europaea in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FT6
- Type
- protein
- Length
- 208 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C554
- UniProt
- Q57142
- Ligands
- HEC, DTN, SO3, PO4
- Pockets
- 1 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C554 | protein | 208 | 38% helix, 4% strand | Q57142 |
Ligands and binding sites
- HEC · Heme C · ligand · 4 copies · chains A
- DTN · Dithionite · ligand · chains A
- SO3 · Sulfite ion · ion · chains A
- PO4 · Phosphate ion · ion · 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 | 1187 | 0.84 | 0.85 | 103 | HEC, DTN |
Modifications
Observed in the structure: 8 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 Q57142
- Elsewhere: RCSB PDB 1FT6 · PDBe 1FT6 · UniProt Q57142
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