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 | 16 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12237326","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 915 |
| Chain | Residue | Details |
| A | ASP141 | metal ligand |
| A | LYS144 | proton shuttle (general acid/base) |
| A | ASP169 | metal ligand |
| A | ASN170 | metal ligand |
| A | GLU199 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 915 |
| Chain | Residue | Details |
| B | ASP141 | metal ligand |
| B | LYS144 | proton shuttle (general acid/base) |
| B | ASP169 | metal ligand |
| B | ASN170 | metal ligand |
| B | GLU199 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 915 |
| Chain | Residue | Details |
| C | ASP141 | metal ligand |
| C | LYS144 | proton shuttle (general acid/base) |
| C | ASP169 | metal ligand |
| C | ASN170 | metal ligand |
| C | GLU199 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 915 |
| Chain | Residue | Details |
| D | ASP141 | metal ligand |
| D | LYS144 | proton shuttle (general acid/base) |
| D | ASP169 | metal ligand |
| D | ASN170 | metal ligand |
| D | GLU199 | electrostatic stabiliser |
