3a7e Summary


Crystal structure of human COMT complexed with SAM and 3,5-dinitrocatechol

A publication describing this structure is not available. The depositing authors are Tsuji, E.search

This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 2009.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of Catechol O-methyltransferase. This molecule has the UniProt identifier P21964 (COMT_HUMAN)search. The sample contained 216 residues which is < 90% of the natural sequence. Out of 216 residues 212 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Catechol O-methyltransferase P21964 (51-264) (COMT_HUMAN)search Homo sapienssearch < 90% 216 98%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P21964 (51 - 264) Catechol O-methyltransferase Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A Vaccinia Virus protein VP39search O-methyltransferasesearch

Chain ID Molecular function (GO) Biological process (GO)
A (P21964) magnesium ion bindingsearch catechol O-methyltransferase activitysearch O-methyltransferase activitysearch neurotransmitter catabolic processsearch catecholamine metabolic processsearch

Chain InterPro annotation
A O-methyltransferase, family 3search Catechol O-methyltransferase, eukaryoticsearch Catechol O-methyltransferasesearch S-adenosyl-L-methionine-dependent methyltransferase-likesearch