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Cytochrome P450SP alpha (CYP152B1) mutant F288G

Analyse Cytochrome P450SP alpha (CYP152B1) mutant F288G in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3AWP
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: 5 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fatty acid alpha-hydroxylase (EC 1.11.2.4)	protein	407	53% helix, 12% strand	O24782

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
PLM · Palmitic acid · ligand · chains A
MRD · (4R)-2-methylpentane-2,4-diol · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 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	1024	0.85	0.85	74	HEM, PLM, MRD
2	62	0.30	0.75	16	empty
3	56	0.29	0.75	13	empty
4	61	0.27	0.73	14	empty
5	53	0.26	0.73	15	empty

Compared structures

3AWP · Cytochrome P450SP alpha (CYP152B1) mutant F288G · 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 3AWP · PDBe 3AWP · UniProt O24782

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