MolNFT v1 · #58220 · protein
Cytochrome P450SP alpha (CYP152B1) mutant L78F
3AWQ · Fatty acid alpha-hydroxylase: “Cytochrome P450SP alpha (CYP152B1) mutant L78F”. X-ray diffraction, 2 ligands (HEM, PLM), 4 pockets (best druggability 0.86). MolNFT v1 #58220 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 3AWQ
- Type
- protein
- Length
- 407 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty acid alpha-hydroxylase
- EC
- 1.11.2.4
- UniProt
- O24782
- Ligands
- HEM, PLM
- Pockets
- 4 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fatty acid alpha-hydroxylase (EC 1.11.2.4) | protein | 407 | 51% helix, 12% strand | O24782 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 913 | 0.86 | 0.88 | 71 | HEM, PLM |
| 2 | 90 | 0.35 | 0.74 | 17 | empty |
| 3 | 59 | 0.28 | 0.74 | 16 | empty |
| 4 | 51 | 0.25 | 0.73 | 11 | empty |
Compared structures
- 3AWQ · Cytochrome P450SP alpha (CYP152B1) mutant L78F · 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 O24782
- Elsewhere: RCSB PDB 3AWQ · PDBe 3AWQ · UniProt O24782
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