4IWW
Computational Design of an Unnatural Amino Acid Metalloprotein with Atomic Level Accuracy
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 |
| B | 0000162 | biological_process | L-tryptophan biosynthetic process |
| B | 0004425 | molecular_function | indole-3-glycerol-phosphate synthase activity |
| B | 0006568 | biological_process | L-tryptophan metabolic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 301 |
| Chain | Residue |
| B | LYS53 |
| B | GLY233 |
| B | SER234 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| A | LYS53 |
| A | GLY233 |
| A | SER234 |
| A | HOH424 |
| B | ARG171 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 303 |
| Chain | Residue |
| A | ARG43 |
| B | LYS42 |
| A | ARG36 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 304 |
| Chain | Residue |
| A | ARG3 |
| A | ARG97 |
| A | ILE168 |
| B | LYS242 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 305 |
| Chain | Residue |
| A | ARG64 |
| A | ASP65 |
| B | SER21 |
| B | ARG23 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 306 |
| Chain | Residue |
| A | LYS115 |
| A | GLU116 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO A 307 |
| Chain | Residue |
| A | BP5133 |
| A | GLU159 |
| A | ASP184 |
| A | HOH416 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 301 |
| Chain | Residue |
| A | LYS242 |
| B | ARG3 |
| B | ARG97 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 302 |
| Chain | Residue |
| A | SER21 |
| A | ARG23 |
| A | HOH417 |
| B | ARG64 |
| B | ASP65 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 303 |
| Chain | Residue |
| A | LYS42 |
| B | ARG36 |
| B | PHE40 |
| B | ARG43 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO B 304 |
| Chain | Residue |
| B | BP5133 |
| B | GLU159 |
| B | ASP184 |
| B | HOH415 |
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 | MET110 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU163 | activator, hydrogen bond acceptor, increase nucleophilicity |
| A | ASP184 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity |
| A | SER214 | electrostatic stabiliser |
| A | GLU215 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 252 |
| Chain | Residue | Details |
| B | GLU51 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity, proton acceptor, proton donor |
| B | LYS53 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| B | MET110 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU163 | activator, hydrogen bond acceptor, increase nucleophilicity |
| B | ASP184 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity |
| B | SER214 | electrostatic stabiliser |
| B | GLU215 | electrostatic stabiliser, hydrogen bond donor |
