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Structure of human type B cytochrome B5
Analyse Structure of human type B cytochrome B5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NER
- Type
- protein
- Length
- 181 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome B5 type B
- UniProt
- O43169
- Ligands
- HEM, MG, SO4
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome B5 type B | protein | 90 | 33% helix, 22% strand | O43169 |
| B | Cytochrome B5 type B | protein | 91 | 35% helix, 22% strand | O43169 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · chains B
- SO4 · Sulfate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 381 | 0.71 | 0.82 | 40 | HEM, SO4 |
| 2 | 104 | 0.63 | 0.87 | 19 | HEM |
Interfaces
1 interface between chains.
- A–B · 245 Ų buried · 7 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 O43169
- Elsewhere: RCSB PDB 3NER · PDBe 3NER · UniProt O43169
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