1K0G
THE CRYSTAL STRUCTURE OF AMINODEOXYCHORISMATE SYNTHASE FROM PHOSPHATE GROWN CRYSTALS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000162 | biological_process | L-tryptophan biosynthetic process |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0008153 | biological_process | 4-aminobenzoate biosynthetic process |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009356 | cellular_component | aminodeoxychorismate synthase complex |
| A | 0009396 | biological_process | folic acid-containing compound biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| A | 0046656 | biological_process | folic acid biosynthetic process |
| A | 0046820 | molecular_function | 4-amino-4-deoxychorismate synthase activity |
| A | 0046982 | molecular_function | protein heterodimerization activity |
| A | 0120284 | molecular_function | tryptophan binding |
| B | 0000162 | biological_process | L-tryptophan biosynthetic process |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0008153 | biological_process | 4-aminobenzoate biosynthetic process |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009356 | cellular_component | aminodeoxychorismate synthase complex |
| B | 0009396 | biological_process | folic acid-containing compound biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| B | 0046656 | biological_process | folic acid biosynthetic process |
| B | 0046820 | molecular_function | 4-amino-4-deoxychorismate synthase activity |
| B | 0046982 | molecular_function | protein heterodimerization activity |
| B | 0120284 | molecular_function | tryptophan binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 701 |
| Chain | Residue |
| A | TYR112 |
| A | HOH1222 |
| A | ASP113 |
| A | ARG116 |
| A | ALA125 |
| A | ILE379 |
| A | ASP380 |
| A | ARG386 |
| A | ARG387 |
| A | HOH1041 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 702 |
| Chain | Residue |
| B | ASP113 |
| B | ARG116 |
| B | ALA125 |
| B | ILE379 |
| B | ASP380 |
| B | ARG386 |
| B | ARG387 |
| B | HOH1064 |
| B | HOH1075 |
| B | HOH1372 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE TRP A 601 |
| Chain | Residue |
| A | LEU34 |
| A | HIS35 |
| A | SER36 |
| A | TYR43 |
| A | SER44 |
| A | ARG45 |
| A | PHE46 |
| A | PRO240 |
| A | PHE241 |
| A | SER242 |
| A | ILE394 |
| A | HOH1076 |
| A | HOH1137 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE TRP B 602 |
| Chain | Residue |
| B | LEU34 |
| B | HIS35 |
| B | SER36 |
| B | TYR43 |
| B | SER44 |
| B | ARG45 |
| B | PHE46 |
| B | PRO240 |
| B | PHE241 |
| B | SER242 |
| B | ILE394 |
| B | HOH1071 |
| B | HOH1172 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"N6-(4-deoxychorismate)-lysine intermediate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11841211","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 283 |
| Chain | Residue | Details |
| A | GLU258 | activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | LYS274 | activator, hydrogen bond donor, nucleofuge, nucleophile, polar/non-polar interaction |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 283 |
| Chain | Residue | Details |
| B | GLU258 | activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | LYS274 | activator, hydrogen bond donor, nucleofuge, nucleophile, polar/non-polar interaction |
