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Crystal structure of human 108M catechol O-methyltransferase bound with S-adenosylmethionine and inhibitor dinitrocatechol

Analyse Crystal structure of human 108M catechol O-methyltransferase bound with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BWY
Type: protein
Length: 214 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Comt protein
EC: 2.1.1.6
UniProt: Q6ICE6
Ligands: SAM, DNC, MG
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Comt protein (EC 2.1.1.6)	protein	214	48% helix, 23% strand	Q6ICE6

Ligands and binding sites

SAM · S-adenosylmethionine · ligand · chains A
DNC · 3,5-dinitrocatechol · ligand · chains A
MG · Magnesium ion · metal · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	148	0.61	0.84	33	SAM, DNC

Compared structures

3BWY · Crystal Structure of Human 108M Catechol O-methyltransferase bound with… · 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 Q6ICE6
Elsewhere: RCSB PDB 3BWY · PDBe 3BWY · UniProt Q6ICE6

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