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The crystal structure of CYP199A4 bound to 4-n-propylbenzoic acid

Analyse The crystal structure of CYP199A4 bound to 4-n-propylbenzoic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7R8S
Type: protein
Length: 393 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.366
Source: Rhodopseudomonas palustris (strain HaA2)
Molecule: Cytochrome P450
UniProt: Q2IU02
Ligands: HEM, 8ZU, CL
Pockets: 2 · best druggability 0.85

Structure

x-ray diffraction · resolution 1.366 · 1 distinct chain · 50% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450	protein	393	50% helix, 13% strand	Q2IU02

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
8ZU · 4-propylbenzoic acid · ligand · chains A
CL · Chloride ion · ion · 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	346	0.85	0.94	48	HEM, 8ZU
2	130	0.42	0.76	21	empty

Compared structures

7R8S · The crystal structure of CYP199A4 bound to 4-N-propylbenzoic 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 Q2IU02
Elsewhere: RCSB PDB 7R8S · PDBe 7R8S · UniProt Q2IU02

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