MolNFT v1 · #101946 · protein
Crystal structure of cytochrome B561
4O6Y · Probable transmembrane ascorbate ferrireductase 2: “Crystal structure of cytochrome B561”. X-ray diffraction, 2 ligands (HEM, SO4), 6 pockets (best druggability 0.79). MolNFT v1 #101946 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4O6Y
- Type
- protein
- Length
- 421 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable transmembrane ascorbate ferrireductase 2
- EC
- 1.16.5.1
- UniProt
- Q9SWS1
- Ligands
- HEM, SO4
- Pockets
- 6 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable transmembrane ascorbate ferrireductase 2 (EC 1.16.5.1) | protein | 210 | 82% helix, 0% strand | Q9SWS1 |
| B | Probable transmembrane ascorbate ferrireductase 2 (EC 1.16.5.1) | protein | 211 | 81% helix, 0% strand | Q9SWS1 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 368 | 0.79 | 0.88 | 47 | HEM |
| 2 | 356 | 0.77 | 0.87 | 49 | HEM |
| 3 | 660 | 0.72 | 0.78 | 46 | empty |
| 4 | 210 | 0.71 | 0.87 | 23 | HEM |
| 5 | 205 | 0.68 | 0.86 | 27 | HEM |
Interfaces
1 interface between chains.
- A–B · 1455 Ų buried · 6 hydrogen bonds · protein-protein
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 Q9SWS1
- Elsewhere: RCSB PDB 4O6Y · PDBe 4O6Y · UniProt Q9SWS1
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