5LQJ
Crystal Structure of COMT in complex with 3-cyclopropyl-5-methyl-4-phenyl-1,2,4-triazole
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0006584 | biological_process | catecholamine metabolic process |
A | 0008171 | molecular_function | O-methyltransferase activity |
A | 0016206 | molecular_function | catechol O-methyltransferase activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0006584 | biological_process | catecholamine metabolic process |
B | 0008171 | molecular_function | O-methyltransferase activity |
B | 0016206 | molecular_function | catechol O-methyltransferase activity |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0006584 | biological_process | catecholamine metabolic process |
C | 0008171 | molecular_function | O-methyltransferase activity |
C | 0016206 | molecular_function | catechol O-methyltransferase activity |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0006584 | biological_process | catecholamine metabolic process |
D | 0008171 | molecular_function | O-methyltransferase activity |
D | 0016206 | molecular_function | catechol O-methyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue NA A 301 |
Chain | Residue |
A | VAL183 |
A | ARG184 |
A | SER186 |
A | PHE189 |
A | HOH429 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue 72N A 302 |
Chain | Residue |
D | TYR182 |
A | ALA181 |
A | TYR182 |
C | TYR200 |
D | ASP178 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue NA B 301 |
Chain | Residue |
B | VAL183 |
B | ARG184 |
B | SER186 |
B | PHE189 |
B | HOH425 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue 72N B 302 |
Chain | Residue |
B | LEU61 |
B | VAL62 |
B | ARG85 |
B | LEU87 |
B | THR113 |
B | TYR130 |
B | ASP131 |
B | VAL132 |
B | LEU135 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue CL B 303 |
Chain | Residue |
B | TYR68 |
B | CYS69 |
B | GLY70 |
B | TYR71 |
B | SER72 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue NA C 301 |
Chain | Residue |
C | VAL183 |
C | ARG184 |
C | SER186 |
C | PHE189 |
C | HOH428 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue 72N C 302 |
Chain | Residue |
A | TYR200 |
B | LEU148 |
B | ASP178 |
B | TYR182 |
C | ALA181 |
C | TYR182 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue 72N C 303 |
Chain | Residue |
A | VAL204 |
C | ARG184 |
C | HIS193 |
C | SER195 |
C | HOH401 |
C | HOH405 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue K D 301 |
Chain | Residue |
D | VAL183 |
D | ARG184 |
D | SER186 |
D | PHE189 |
D | HOH427 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue 72N D 302 |
Chain | Residue |
D | VAL62 |
D | ARG85 |
D | LEU87 |
D | THR113 |
D | TYR130 |
D | VAL132 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | MET1-GLY2 | |
B | MET1-GLY2 | |
C | MET1-GLY2 | |
D | MET1-GLY2 |
site_id | SWS_FT_FI2 |
Number of Residues | 64 |
Details | TRANSMEM: Helical; Signal-anchor for type II membrane protein => ECO:0000255 |
Chain | Residue | Details |
A | ASP3-PRO19 | |
B | ASP3-PRO19 | |
C | ASP3-PRO19 | |
D | ASP3-PRO19 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000269|PubMed:12237326 |
Chain | Residue | Details |
A | ARG85 | |
C | LEU115 | |
C | ASP133 | |
C | ARG184 | |
D | ARG85 | |
D | LEU115 | |
D | ASP133 | |
D | ARG184 | |
A | LEU115 | |
A | ASP133 | |
A | ARG184 | |
B | ARG85 | |
B | LEU115 | |
B | ASP133 | |
B | ARG184 | |
C | ARG85 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019 |
Chain | Residue | Details |
A | GLY107 | |
D | GLY107 | |
D | THR134 | |
D | LYS162 | |
A | THR134 | |
A | LYS162 | |
B | GLY107 | |
B | THR134 | |
B | LYS162 | |
C | GLY107 | |
C | THR134 | |
C | LYS162 |
site_id | SWS_FT_FI5 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | LEU160 | |
C | SER187 | |
C | TYR212 | |
C | GLN213 | |
D | LEU160 | |
D | SER187 | |
D | TYR212 | |
D | GLN213 | |
A | SER187 | |
A | TYR212 | |
A | GLN213 | |
B | LEU160 | |
B | SER187 | |
B | TYR212 | |
B | GLN213 | |
C | LEU160 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 915 |
Chain | Residue | Details |
A | ARG184 | metal ligand |
A | SER187 | proton shuttle (general acid/base) |
A | TYR212 | metal ligand |
A | GLN213 | metal ligand |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 915 |
Chain | Residue | Details |
B | ARG184 | metal ligand |
B | SER187 | proton shuttle (general acid/base) |
B | TYR212 | metal ligand |
B | GLN213 | metal ligand |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 915 |
Chain | Residue | Details |
C | ARG184 | metal ligand |
C | SER187 | proton shuttle (general acid/base) |
C | TYR212 | metal ligand |
C | GLN213 | metal ligand |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 915 |
Chain | Residue | Details |
D | ARG184 | metal ligand |
D | SER187 | proton shuttle (general acid/base) |
D | TYR212 | metal ligand |
D | GLN213 | metal ligand |