4A2S
Structure of the engineered retro-aldolase RA95.5
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 | 15 |
| Details | BINDING SITE FOR RESIDUE 3NK A 1083 |
| Chain | Residue |
| A | TRP8 |
| A | LEU159 |
| A | ASN161 |
| A | PHE180 |
| A | PHE184 |
| A | 3NK1210 |
| A | HOH2107 |
| A | LEU9 |
| A | LYS83 |
| A | PHE89 |
| A | SER110 |
| A | ASP111 |
| A | PHE112 |
| A | ILE133 |
| A | LYS135 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 3NK A 1210 |
| Chain | Residue |
| A | TRP8 |
| A | SER58 |
| A | MET182 |
| A | PHE184 |
| A | LYS210 |
| A | 3NK1083 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 252 |
| Chain | Residue | Details |
| A | TYR51 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity, proton acceptor, proton donor |
| A | SER53 | 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 | PHE180 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity |
| A | LYS210 | electrostatic stabiliser |
| A | LEU211 | electrostatic stabiliser, hydrogen bond donor |
