3TC6
Crystal Structure of Engineered Protein. Northeast Structural Genomics Consortium Target OR63.
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 | 9 |
Details | BINDING SITE FOR RESIDUE PO4 A 301 |
Chain | Residue |
A | ARG97 |
A | ASN164 |
A | ARG171 |
A | SER235 |
A | ARG238 |
A | ASN239 |
A | LYS242 |
A | HOH649 |
A | HOH689 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 A 302 |
Chain | Residue |
A | LYS53 |
A | ARG182 |
A | ALA211 |
A | GLY233 |
A | SER234 |
A | HOH524 |
A | HOH573 |
A | HOH625 |
A | HOH634 |
A | HOH658 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A 303 |
Chain | Residue |
A | ARG36 |
A | GLU39 |
A | LYS42 |
A | ARG43 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 A 304 |
Chain | Residue |
A | SER25 |
A | GLN27 |
A | ASP162 |
A | GLU163 |
A | ASN193 |
A | LYS196 |
A | HOH660 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PEG A 401 |
Chain | Residue |
A | TRP8 |
A | GLU185 |
A | THR186 |
A | LEU187 |
A | ASN204 |
A | HOH563 |
A | HOH675 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PEG A 402 |
Chain | Residue |
A | ILE201 |
Functional Information from PROSITE/UniProt
site_id | PS00614 |
Number of Residues | 15 |
Details | IGPS Indole-3-glycerol phosphate synthase signature. IIaEYKRKSPSgld....V |
Chain | Residue | Details |
A | ILE48-VAL62 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 252 |
Chain | Residue | Details |
A | GLU51 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity, proton acceptor, proton donor |
A | LYS53 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
A | SER110 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | VAL159 | activator, hydrogen bond acceptor, increase nucleophilicity |
A | GLU180 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity |
A | ILE210 | electrostatic stabiliser |
A | ALA211 | electrostatic stabiliser, hydrogen bond donor |