4P7G
Rat apo-COMT, phosphate bound
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 | 8 |
| Details | binding site for residue PO4 A 300 |
| Chain | Residue |
| A | LYS89 |
| A | ALA110 |
| A | TYR111 |
| A | CYS112 |
| A | GLY113 |
| A | TYR114 |
| A | SER115 |
| A | ASP184 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue K A 301 |
| Chain | Residue |
| A | ARG227 |
| A | SER229 |
| A | PHE232 |
| B | GLU242 |
| B | HOH419 |
| A | VAL226 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 B 300 |
| Chain | Residue |
| B | LYS89 |
| B | TYR111 |
| B | CYS112 |
| B | GLY113 |
| B | TYR114 |
| B | SER115 |
| B | ASP184 |
| B | HOH405 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue K B 301 |
| Chain | Residue |
| A | GLU242 |
| A | HOH428 |
| B | VAL226 |
| B | ARG227 |
| B | SER229 |
| B | PHE232 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue PO4 C 300 |
| Chain | Residue |
| C | LYS89 |
| C | TYR111 |
| C | CYS112 |
| C | GLY113 |
| C | TYR114 |
| C | SER115 |
| C | ASP184 |
| C | HOH403 |
| C | HOH423 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 D 300 |
| Chain | Residue |
| D | LYS89 |
| D | ALA110 |
| D | TYR111 |
| D | CYS112 |
| D | GLY113 |
| D | TYR114 |
| D | SER115 |
| D | ASP184 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000269|PubMed:12237326 |
| Chain | Residue | Details |
| D | VAL85 | |
| D | SER115 | |
| D | GLU133 | |
| D | ASP184 | |
| A | VAL85 | |
| A | SER115 | |
| A | GLU133 | |
| A | ASP184 | |
| B | VAL85 | |
| B | SER115 | |
| B | GLU133 | |
| B | ASP184 | |
| C | VAL85 | |
| C | SER115 | |
| C | GLU133 | |
| C | ASP184 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019 |
| Chain | Residue | Details |
| B | MET134 | |
| B | SER162 | |
| C | GLU107 | |
| C | MET134 | |
| C | SER162 | |
| D | GLU107 | |
| D | MET134 | |
| D | SER162 | |
| A | SER162 | |
| B | GLU107 | |
| A | GLU107 | |
| A | MET134 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLU242 | |
| B | GLY160 | |
| B | LYS187 | |
| B | ASP212 | |
| B | ASN213 | |
| B | GLU242 | |
| C | GLY160 | |
| C | LYS187 | |
| C | ASP212 | |
| C | ASN213 | |
| C | GLU242 | |
| D | GLY160 | |
| D | LYS187 | |
| D | ASP212 | |
| D | ASN213 | |
| D | GLU242 | |
| A | ASP212 | |
| A | ASN213 | |
| A | GLY160 | |
| A | LYS187 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
| Chain | Residue | Details |
| B | SER264 | |
| C | SER259 | |
| C | SER260 | |
| C | SER264 | |
| D | SER259 | |
| D | SER260 | |
| D | SER264 | |
| A | SER260 | |
| A | SER264 | |
| B | SER259 | |
| B | SER260 | |
| A | SER259 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 915 |
| Chain | Residue | Details |
| A | ASP184 | metal ligand |
| A | LYS187 | proton shuttle (general acid/base) |
| A | ASP212 | metal ligand |
| A | ASN213 | metal ligand |
| A | GLU242 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 915 |
| Chain | Residue | Details |
| B | ASP184 | metal ligand |
| B | LYS187 | proton shuttle (general acid/base) |
| B | ASP212 | metal ligand |
| B | ASN213 | metal ligand |
| B | GLU242 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 915 |
| Chain | Residue | Details |
| C | ASP184 | metal ligand |
| C | LYS187 | proton shuttle (general acid/base) |
| C | ASP212 | metal ligand |
| C | ASN213 | metal ligand |
| C | GLU242 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 915 |
| Chain | Residue | Details |
| D | ASP184 | metal ligand |
| D | LYS187 | proton shuttle (general acid/base) |
| D | ASP212 | metal ligand |
| D | ASN213 | metal ligand |
| D | GLU242 | electrostatic stabiliser |
