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Cytochrome P450SP alpha (CYP152B1) mutant R241E

Analyse Cytochrome P450SP alpha (CYP152B1) mutant R241E in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3VNO
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: 2 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fatty acid alpha-hydroxylase (EC 1.11.2.4)	protein	407	50% helix, 12% strand	O24782

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A

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

Pockets

2 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	1022	0.85	0.86	71	HEM, MPD
2	65	0.28	0.73	15	empty

Compared structures

3VNO · Cytochrome P450SP alpha (CYP152B1) mutant R241E · 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 3VNO · PDBe 3VNO · UniProt O24782

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