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 | |
D | SER305 | |
D | ASP367 | |
D | SER368 | |
A | ASP367 | |
A | SER368 | |
B | SER305 | |
B | ASP367 | |
B | SER368 | |
C | SER305 | |
C | ASP367 | |
C | SER368 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ecf |
Chain | Residue | Details |
A | GLY102 | |
A | CYS1 | |
A | ASN101 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ecf |
Chain | Residue | Details |
B | GLY102 | |
B | CYS1 | |
B | ASN101 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ecf |
Chain | Residue | Details |
C | GLY102 | |
C | CYS1 | |
C | ASN101 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ecf |
Chain | Residue | Details |
D | GLY102 | |
D | CYS1 | |
D | ASN101 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ecf |
Chain | Residue | Details |
A | SER345 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ecf |
Chain | Residue | Details |
B | SER345 |
site_id | CSA7 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ecf |
Chain | Residue | Details |
C | SER345 |
site_id | CSA8 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ecf |
Chain | Residue | Details |
D | SER345 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 214 |
Chain | Residue | Details |
A | GLY2 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
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 |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 214 |
Chain | Residue | Details |
B | GLY2 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
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 |
site_id | MCSA3 |
Number of Residues | 5 |
Details | M-CSA 214 |
Chain | Residue | Details |
C | GLY2 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
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 |
site_id | MCSA4 |
Number of Residues | 5 |
Details | M-CSA 214 |
Chain | Residue | Details |
D | GLY2 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
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 |