Research workbench
2.4A resolution structure of bovine cytochrome B5 (S71L)
Analyse 2.4A resolution structure of bovine cytochrome B5 (S71L) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HIN
- Type
- protein
- Length
- 327 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome B5
- UniProt
- P00171
- Ligands
- HEM, CU
- Pockets
- 5 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome B5 | protein | 81 | 40% helix, 23% strand | P00171 |
| B, C, D | Cytochrome B5 | protein | 82 | 39% helix, 23% strand | P00171 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, C, D, B
- CU · Copper (II) ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 685 | 0.70 | 0.77 | 72 | HEM |
| 2 | 128 | 0.57 | 0.83 | 19 | HEM |
| 3 | 110 | 0.54 | 0.82 | 19 | HEM |
| 4 | 62 | 0.26 | 0.72 | 7 | empty |
| 5 | 52 | 0.25 | 0.73 | 18 | empty |
Interfaces
5 interfaces between chains.
- C–D · 245 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 239 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 111 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 69 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 22 Ų buried · 0 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 P00171
- Elsewhere: RCSB PDB 4HIN · PDBe 4HIN · UniProt P00171
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