4A29
Structure of the engineered retro-aldolase RA95.0
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000162 | biological_process | tryptophan biosynthetic process |
| A | 0004425 | molecular_function | indole-3-glycerol-phosphate synthase activity |
| A | 0004640 | molecular_function | phosphoribosylanthranilate isomerase activity |
| A | 0006568 | biological_process | tryptophan metabolic process |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 3NK A 299 |
| Chain | Residue |
| A | MET180 |
| A | ARG182 |
| A | ASP183 |
| A | GLY187 |
| A | LYS210 |
| A | MLT300 |
| A | HOH2303 |
| A | HOH2340 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MLT A 300 |
| Chain | Residue |
| A | SER56 |
| A | SER58 |
| A | PHE89 |
| A | ARG182 |
| A | GLY212 |
| A | SER233 |
| A | SER234 |
| A | 3NK299 |
| A | HOH2160 |
| A | HOH2175 |
| A | HOH2304 |
| A | GLU53 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 252 |
| Chain | Residue | Details |
| A | VAL51 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity, proton acceptor, proton donor |
| A | GLU53 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| A | SER110 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | LEU159 | activator, hydrogen bond acceptor, increase nucleophilicity |
| A | MET180 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity |
| A | LYS210 | electrostatic stabiliser |
| A | LEU211 | electrostatic stabiliser, hydrogen bond donor |
