1ECJ
ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE COMPLEXED WITH 2 AMP PER TETRAMER
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004044 | molecular_function | amidophosphoribosyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0006541 | biological_process | glutamine metabolic process |
| A | 0009113 | biological_process | purine nucleobase biosynthetic process |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0097216 | molecular_function | guanosine tetraphosphate binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004044 | molecular_function | amidophosphoribosyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| B | 0006541 | biological_process | glutamine metabolic process |
| B | 0009113 | biological_process | purine nucleobase biosynthetic process |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0097216 | molecular_function | guanosine tetraphosphate binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004044 | molecular_function | amidophosphoribosyltransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006164 | biological_process | purine nucleotide biosynthetic process |
| C | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| C | 0006541 | biological_process | glutamine metabolic process |
| C | 0009113 | biological_process | purine nucleobase biosynthetic process |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0097216 | molecular_function | guanosine tetraphosphate binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004044 | molecular_function | amidophosphoribosyltransferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006164 | biological_process | purine nucleotide biosynthetic process |
| D | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| D | 0006541 | biological_process | glutamine metabolic process |
| D | 0009113 | biological_process | purine nucleobase biosynthetic process |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0097216 | molecular_function | guanosine tetraphosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AMP A 505 |
| Chain | Residue |
| A | TYR74 |
| A | PHE254 |
| A | ASP366 |
| A | ASP367 |
| A | SER368 |
| A | VAL370 |
| A | ARG371 |
| A | GLY372 |
| A | THR374 |
| A | ASP408 |
| A | MET409 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AMP C 505 |
| Chain | Residue |
| C | TYR74 |
| C | PHE254 |
| C | ASP366 |
| C | ASP367 |
| C | SER368 |
| C | VAL370 |
| C | ARG371 |
| C | GLY372 |
| C | THR374 |
| C | ASP408 |
| C | MET409 |
| site_id | NTA |
| Number of Residues | 1 |
| Details | NTN AMIDOTRANSFERASE ACTIVE SITE. |
| Chain | Residue |
| A | CYS1 |
| site_id | NTB |
| Number of Residues | 1 |
| Details | NTN AMIDOTRANSFERASE ACTIVE SITE. |
| Chain | Residue |
| B | CYS1 |
| site_id | NTC |
| Number of Residues | 1 |
| Details | NTN AMIDOTRANSFERASE ACTIVE SITE. |
| Chain | Residue |
| C | CYS1 |
| site_id | NTD |
| Number of Residues | 1 |
| Details | NTN AMIDOTRANSFERASE ACTIVE SITE. |
| Chain | Residue |
| D | CYS1 |
| site_id | PRA |
| Number of Residues | 2 |
| Details | PHOSPHORIBOSYL TRANSFERASE ACTIVE SITE. THE ACTIVE SITE IN THIS STRUCTURE CONTAINS THE FEEDBACK INHIBITOR AMP IN 2 OF 4 CATALYTIC SITES, ALTHOUGH BINDING IS IN THE ABSENCE OF A DIVALENT METAL ION. ASP 366 AND ASP 367 FUNCTION AS METAL LIGANDS IN THE INHIBITED STATE OF THIS ENZYME, AND ARE THE HALLMARK OF TYPE I PRTASE ENZYMES. |
| Chain | Residue |
| B | ASP366 |
| B | ASP367 |
| site_id | PRB |
| Number of Residues | 2 |
| Details | PHOSPHORIBOSYL TRANSFERASE ACTIVE SITE. THE ACTIVE SITE IN THIS STRUCTURE CONTAINS THE FEEDBACK INHIBITOR AMP IN 2 OF 4 CATALYTIC SITES, ALTHOUGH BINDING IS IN THE ABSENCE OF A DIVALENT METAL ION. ASP 366 AND ASP 367 FUNCTION AS METAL LIGANDS IN THE INHIBITED STATE OF THIS ENZYME, AND ARE THE HALLMARK OF TYPE I PRTASE ENZYMES. |
| Chain | Residue |
| C | ASP366 |
| C | ASP367 |
| site_id | PRC |
| Number of Residues | 2 |
| Details | PHOSPHORIBOSYL TRANSFERASE ACTIVE SITE. THE ACTIVE SITE IN THIS STRUCTURE CONTAINS THE FEEDBACK INHIBITOR AMP IN 2 OF 4 CATALYTIC SITES, ALTHOUGH BINDING IS IN THE ABSENCE OF A DIVALENT METAL ION. ASP 366 AND ASP 367 FUNCTION AS METAL LIGANDS IN THE INHIBITED STATE OF THIS ENZYME, AND ARE THE HALLMARK OF TYPE I PRTASE ENZYMES. |
| Chain | Residue |
| D | ASP366 |
| D | ASP367 |
| site_id | PRT |
| Number of Residues | 2 |
| Details | PHOSPHORIBOSYL TRANSFERASE ACTIVE SITE. THE ACTIVE SITE IN THIS STRUCTURE CONTAINS THE FEEDBACK INHIBITOR AMP IN 2 OF 4 CATALYTIC SITES, ALTHOUGH BINDING IS IN THE ABSENCE OF A DIVALENT METAL ION. ASP 366 AND ASP 367 FUNCTION AS METAL LIGANDS IN THE INHIBITED STATE OF THIS ENZYME, AND ARE THE HALLMARK OF TYPE I PRTASE ENZYMES. |
| Chain | Residue |
| A | ASP366 |
| A | ASP367 |
Functional Information from PROSITE/UniProt
| site_id | PS00103 |
| Number of Residues | 13 |
| Details | PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLLVDDSIVRGtT |
| Chain | Residue | Details |
| A | VAL362-THR374 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000269|PubMed:7037784 |
| Chain | Residue | Details |
| A | GLY2 | |
| B | GLY2 | |
| C | GLY2 | |
| D | GLY2 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01931 |
| Chain | Residue | Details |
| A | SER305 | |
| A | ASP367 | |
| A | SER368 | |
| B | SER305 | |
| B | ASP367 | |
| B | SER368 | |
| C | SER305 | |
| C | ASP367 | |
| C | SER368 | |
| D | SER305 | |
| D | ASP367 | |
| D | SER368 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 214 |
| Chain | Residue | Details |
| A | GLN28 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | GLY102 | electrostatic stabiliser, hydrogen bond donor |
| A | ASN103 | electrostatic stabiliser, hydrogen bond donor |
| A | PHE259 | electrostatic stabiliser, hydrogen bond donor |
| A | GLY2 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 214 |
| Chain | Residue | Details |
| B | GLN28 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| B | GLY102 | electrostatic stabiliser, hydrogen bond donor |
| B | ASN103 | electrostatic stabiliser, hydrogen bond donor |
| B | PHE259 | electrostatic stabiliser, hydrogen bond donor |
| B | GLY2 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 214 |
| Chain | Residue | Details |
| C | GLN28 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| C | GLY102 | electrostatic stabiliser, hydrogen bond donor |
| C | ASN103 | electrostatic stabiliser, hydrogen bond donor |
| C | PHE259 | electrostatic stabiliser, hydrogen bond donor |
| C | GLY2 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 214 |
| Chain | Residue | Details |
| D | GLN28 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| D | GLY102 | electrostatic stabiliser, hydrogen bond donor |
| D | ASN103 | electrostatic stabiliser, hydrogen bond donor |
| D | PHE259 | electrostatic stabiliser, hydrogen bond donor |
| D | GLY2 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
