4LNY
Crystal Structure of Engineered Protein, Northeast Structural Genomics Consortium Target OR422
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000162 | biological_process | L-tryptophan biosynthetic process |
| A | 0004425 | molecular_function | indole-3-glycerol-phosphate synthase activity |
| A | 0006568 | biological_process | L-tryptophan metabolic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CD A 301 |
| Chain | Residue |
| A | GLU143 |
| A | SER214 |
| A | GLU218 |
| A | CL307 |
| A | HOH531 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD A 302 |
| Chain | Residue |
| A | GLU68 |
| A | GLU188 |
| A | HOH533 |
| A | HOH557 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CD A 303 |
| Chain | Residue |
| A | ASP183 |
| A | GLU185 |
| A | CL309 |
| A | HOH554 |
| A | HOH595 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CD A 304 |
| Chain | Residue |
| A | ASP65 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CD A 305 |
| Chain | Residue |
| A | ASP162 |
| A | ASP165 |
| A | HOH612 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CD A 306 |
| Chain | Residue |
| A | GLU147 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CL A 307 |
| Chain | Residue |
| A | GLU143 |
| A | LYS191 |
| A | GLY212 |
| A | ILE213 |
| A | SER214 |
| A | GLU218 |
| A | CD301 |
| A | CL308 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 308 |
| Chain | Residue |
| A | GLY212 |
| A | ILE213 |
| A | ALA233 |
| A | CL307 |
| A | HOH501 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 309 |
| Chain | Residue |
| A | LYS71 |
| A | SER102 |
| A | CD303 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 310 |
| Chain | Residue |
| A | LYS245 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 311 |
| Chain | Residue |
| A | GLU147 |
| A | ILE189 |
| A | LYS191 |
| A | HOH608 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 252 |
| Chain | Residue | Details |
| A | LYS55 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity, proton acceptor, proton donor |
| A | PRO57 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| A | GLN118 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ARG175 | activator, hydrogen bond acceptor, increase nucleophilicity |
| A | LYS196 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity |
| A | PHE230 | electrostatic stabiliser |
| A | VAL231 | electrostatic stabiliser, hydrogen bond donor |
