Research workbench

Cytochrome P450SP alpha (CYP152B1) wild-type with palmitic acid

Analyse Cytochrome P450SP alpha (CYP152B1) wild-type with palmitic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3AWM
Type: protein
Length: 407 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.65
Source: Sphingomonas paucimobilis
Molecule: Fatty acid alpha-hydroxylase
EC: 1.11.2.4
UniProt: O24782
Ligands: HEM, PLM
Pockets: 4 · best druggability 0.85

Structure

x-ray diffraction · resolution 1.65 · 1 distinct chain · 52% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fatty acid alpha-hydroxylase (EC 1.11.2.4)	protein	407	52% 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 · 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	965	0.85	0.85	69	HEM, PLM, MRD
2	105	0.37	0.74	18	empty
3	63	0.29	0.74	16	empty
4	66	0.28	0.73	16	empty

Compared structures

3AWM · Cytochrome P450SP alpha (CYP152B1) wild-type with palmitic acid · 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 3AWM · PDBe 3AWM · UniProt O24782

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.