MolNFT v1 · #82652 · protein

Cytochrome P450SP alpha (CYP152B1) mutant A245H

3VTJ · Fatty acid alpha-hydroxylase: “Cytochrome P450SP alpha (CYP152B1) mutant A245H”. X-ray diffraction, 1 ligand (HEM), 4 pockets (best druggability 0.85). MolNFT v1 #82652 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3VTJ
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
Pockets: 4 · best druggability 0.85

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

HEM · Protoporphyrin IX containing Fe · ligand · chains A

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	841	0.85	0.87	69	HEM
2	79	0.31	0.73	16	empty
3	60	0.30	0.75	12	empty
4	67	0.29	0.74	18	empty

Compared structures

3VTJ · Cytochrome P450SP alpha (CYP152B1) mutant A245H · 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 3VTJ · PDBe 3VTJ · UniProt O24782

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