1K0G
THE CRYSTAL STRUCTURE OF AMINODEOXYCHORISMATE SYNTHASE FROM PHOSPHATE GROWN CRYSTALS
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000162 | biological_process | tryptophan biosynthetic process |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0008153 | biological_process | para-aminobenzoic acid 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 | tryptophan biosynthetic process |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0008153 | biological_process | para-aminobenzoic acid 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 | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | GLU258 | |
B | GLU258 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: N6-(4-deoxychorismate)-lysine intermediate |
Chain | Residue | Details |
A | LYS274 | |
B | LYS274 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11841211 |
Chain | Residue | Details |
A | SER36 | |
B | SER36 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | TYR43 | |
A | PRO240 | |
B | TYR43 | |
B | PRO240 |
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 |