5LR6
Crystal Structure of COMT in complex with [3-(2,4-dimethyl-1,3-thiazol-5-yl)-1H-pyrazol-5-yl]-(4-phenylpiperazin-1-yl)methanone
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 | 13 |
| Details | binding site for residue 731 A 301 |
| Chain | Residue |
| A | MET40 |
| A | GLN120 |
| A | HIS142 |
| A | TRP143 |
| A | ARG146 |
| A | GLY66 |
| A | TYR68 |
| A | MET89 |
| A | GLU90 |
| A | ILE91 |
| A | GLY117 |
| A | ALA118 |
| A | SER119 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue NHE A 302 |
| Chain | Residue |
| A | TRP143 |
| A | LYS144 |
| A | ASP145 |
| A | HOH419 |
| C | LYS5 |
| C | GLU6 |
| C | ASN92 |
| C | 731502 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue 731 B 301 |
| Chain | Residue |
| B | GLY66 |
| B | TYR68 |
| B | MET89 |
| B | GLU90 |
| B | ILE91 |
| B | GLY117 |
| B | ALA118 |
| B | SER119 |
| B | HIS142 |
| B | TRP143 |
| D | 731301 |
| D | NHE302 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue NHE B 302 |
| Chain | Residue |
| B | LYS144 |
| B | ASP145 |
| B | HOH404 |
| D | LYS5 |
| D | GLU6 |
| D | TRP38 |
| D | 731301 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue NHE C 501 |
| Chain | Residue |
| A | LYS5 |
| A | GLU6 |
| A | ASN92 |
| A | HOH428 |
| C | TRP143 |
| C | LYS144 |
| C | ASP145 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue 731 C 502 |
| Chain | Residue |
| A | NHE302 |
| C | GLY66 |
| C | TYR68 |
| C | GLU90 |
| C | ILE91 |
| C | GLY117 |
| C | ALA118 |
| C | SER119 |
| C | GLN120 |
| C | HIS142 |
| C | TRP143 |
| C | ARG146 |
| C | HOH613 |
| C | HOH629 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue CL C 503 |
| Chain | Residue |
| C | GLN120 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | binding site for residue 731 D 301 |
| Chain | Residue |
| B | 731301 |
| B | NHE302 |
| D | MET40 |
| D | ASN41 |
| D | GLY66 |
| D | TYR68 |
| D | MET89 |
| D | GLU90 |
| D | ILE91 |
| D | GLY117 |
| D | ALA118 |
| D | SER119 |
| D | GLN120 |
| D | HIS142 |
| D | TRP143 |
| D | HOH436 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue NHE D 302 |
| Chain | Residue |
| B | LYS5 |
| B | GLU6 |
| B | ASN92 |
| B | 731301 |
| D | TRP143 |
| D | LYS144 |
| D | ASP145 |
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 | 27 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| 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 | 4 |
| 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 |
| 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 |
