MolNFT v1 · #35690 · protein
The structure of physarum polycephalum cytochrome B5 reductase
2EIX · NADH-cytochrome B5 reductase: “The structure of physarum polycephalum cytochrome B5 reductase”. X-ray diffraction, 3 ligands (FAD, NA, IOD), 1 pocket (best druggability 0.82). MolNFT v1 #35690 on GenesisL1: 3D structure, binding…
- PDB
- 2EIX
- Type
- protein
- Length
- 486 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADH-cytochrome B5 reductase
- EC
- 1.6.2.2
- UniProt
- Q1HA49
- Ligands
- FAD, NA, IOD
- Pockets
- 1 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | NADH-cytochrome B5 reductase (EC 1.6.2.2) | protein | 243 | 24% helix, 35% strand | Q1HA49 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
- IOD · Iodide ion · ion · 4 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A, B
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 | 1038 | 0.82 | 0.83 | 108 | IOD, FAD, GOL |
Interfaces
1 interface between chains.
- A–B · 681 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 2EIX · The Structure of Physarum polycephalum cytochrome b5 reductase · 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 Q1HA49
- Elsewhere: RCSB PDB 2EIX · PDBe 2EIX · UniProt Q1HA49
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