CATECHOL O-METHYLTRANSFERASE BISUBSTRATE-INHIBITOR COMPLEX
The structure was published by Lerner, C., Ruf, A., Gramlich, V., et al., Jakob-Roetne, R., Borroni, E., and Diederich, F., in 2001 in a paper entitled "X-ray Crystal Structure of a Bisubstrate Inhibitor Bound to the Enzyme Catechol-O-methyltransferase: A Dramatic Effect of Inhibitor Preorganization on Binding Affinity." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.63 Å and deposited in 2001.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of CATECHOL O-METHYLTRANSFERASE, SOLUBLE FORM. This molecule has the UniProt identifier P22734 (COMT_RAT). The sample contained 221 residues which is < 90% of the natural sequence. Out of 221 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):
This entry contains 1 unique UniProt protein: