Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0009058 | biological_process | biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue 1PE A 301 |
Chain | Residue |
A | HIS83 |
A | ARG87 |
A | HIS141 |
A | THR195 |
A | HOH406 |
A | HOH536 |
A | HOH550 |
A | HOH566 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue 1PE A 302 |
Chain | Residue |
A | VAL31 |
A | GLN176 |
A | MET179 |
A | LEU183 |
A | THR187 |
A | ASP210 |
A | THR213 |
A | GLY214 |
A | TYR22 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue CA A 303 |
Chain | Residue |
A | VAL27 |
A | ASP49 |
A | HOH411 |
A | HOH568 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue CA A 304 |
Chain | Residue |
A | GLU108 |
A | ASP199 |
A | HOH500 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue CA A 305 |
Chain | Residue |
A | ASP275 |
A | HOH446 |
A | HOH459 |
A | HOH469 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | SER142 | |
Chain | Residue | Details |
A | HIS259 | |
Chain | Residue | Details |
A | THR76 | |
Chain | Residue | Details |
A | ALA143 | |
A | ASP169 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 602 |
Chain | Residue | Details |
A | SER142 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
A | ALA143 | electrostatic stabiliser |
A | ASP169 | electrostatic stabiliser, modifies pKa |
A | HIS259 | proton acceptor, proton donor |