Research workbench

Crystal structure of the cytochrome P450 monooxygenase aurh (ntermii) from streptomyces thioluteus

Analyse Crystal structure of the cytochrome P450 monooxygenase aurh (ntermii) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3P3O
Type: protein
Length: 416 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450
UniProt: Q70KH6
Ligands: HEM, CL, SO4
Pockets: 3 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450	protein	416	54% helix, 9% strand	Q70KH6

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
CL · Chloride ion · ion · 3 copies · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

3 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	877	0.84	0.86	90	HEM, GOL
2	77	0.47	0.82	16	empty
3	53	0.36	0.80	17	empty

Compared structures

3P3O · Crystal Structure of the Cytochrome P450 Monooxygenase AurH (ntermII) from Streptomyces… · 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 Q70KH6
Elsewhere: RCSB PDB 3P3O · PDBe 3P3O · UniProt Q70KH6

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