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Humanized rat catechol O-methyltransferase in complex with sah and 6- bromo-8-hydroxy-3H-quinazolin-4-one

Analyse Humanized rat catechol O-methyltransferase in complex with sah and 6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5P9U
Type: protein
Length: 214 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Catechol O-methyltransferase
EC: 2.1.1.6
UniProt: P22734
Ligands: SAH, 7JL, MG
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Catechol O-methyltransferase (EC 2.1.1.6)	protein	214	47% helix, 11% strand	P22734

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A
7JL · 6-bromanyl-8-oxidanyl-3~{H}-quinazolin-4-one · ligand · chains A
MG · Magnesium ion · metal · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	337	0.72	0.84	38	empty
2	173	0.55	0.80	36	SAH, 7JL

Compared structures

P22734 · AlphaFold monomer V2.0 prediction for catechol O-methyltransferase (P22734) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P22734
Elsewhere: RCSB PDB 5P9U · PDBe 5P9U · UniProt P22734

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