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 |
A | VAL85 | |
C | SER115 | |
C | GLU133 | |
C | ASP184 | |
D | VAL85 | |
D | SER115 | |
D | GLU133 | |
D | ASP184 | |
A | SER115 | |
A | GLU133 | |
A | ASP184 | |
B | VAL85 | |
B | SER115 | |
B | GLU133 | |
B | ASP184 | |
C | VAL85 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019 |
Chain | Residue | Details |
A | GLU107 | |
D | GLU107 | |
D | MET134 | |
D | SER162 | |
A | MET134 | |
A | SER162 | |
B | GLU107 | |
B | MET134 | |
B | SER162 | |
C | GLU107 | |
C | MET134 | |
C | SER162 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY160 | |
B | GLU242 | |
C | GLY160 | |
C | LYS187 | |
C | ASP212 | |
C | ASN213 | |
C | GLU242 | |
D | GLY160 | |
D | LYS187 | |
D | ASP212 | |
D | ASN213 | |
A | LYS187 | |
D | GLU242 | |
A | ASP212 | |
A | ASN213 | |
A | GLU242 | |
B | GLY160 | |
B | LYS187 | |
B | ASP212 | |
B | ASN213 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
A | SER259 | |
D | SER259 | |
D | SER260 | |
D | SER264 | |
A | SER260 | |
A | SER264 | |
B | SER259 | |
B | SER260 | |
B | SER264 | |
C | SER259 | |
C | SER260 | |
C | SER264 |
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 |