1ECB
ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE COMPLEXED WITH 2 GMP, 1 MG PER SUBUNIT
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 | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 507 |
| Chain | Residue |
| A | ASP366 |
| A | ASP367 |
| A | 5GP505 |
| A | HOH508 |
| A | HOH509 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 507 |
| Chain | Residue |
| B | ASP366 |
| B | ASP367 |
| B | 5GP505 |
| B | HOH508 |
| B | HOH509 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 507 |
| Chain | Residue |
| C | ASP366 |
| C | ASP367 |
| C | 5GP505 |
| C | HOH508 |
| C | HOH509 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 507 |
| Chain | Residue |
| D | ASP366 |
| D | ASP367 |
| D | 5GP505 |
| D | HOH508 |
| D | HOH509 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 5GP A 505 |
| Chain | Residue |
| A | TYR74 |
| A | PHE254 |
| A | TYR258 |
| A | ASP366 |
| A | ASP367 |
| A | SER368 |
| A | VAL370 |
| A | ARG371 |
| A | GLY372 |
| A | THR373 |
| A | THR374 |
| A | 5GP506 |
| A | MG507 |
| A | HOH509 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 5GP A 506 |
| Chain | Residue |
| A | HIS25 |
| A | TYR258 |
| A | ALA260 |
| A | ARG261 |
| A | PRO262 |
| A | ARG275 |
| A | PRO302 |
| A | GLU303 |
| A | THR304 |
| A | LYS326 |
| A | 5GP505 |
| A | HOH508 |
| B | VAL325 |
| B | LYS326 |
| B | ARG328 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 5GP B 505 |
| Chain | Residue |
| B | TYR74 |
| B | PHE254 |
| B | TYR258 |
| B | ASP366 |
| B | ASP367 |
| B | SER368 |
| B | VAL370 |
| B | ARG371 |
| B | GLY372 |
| B | THR373 |
| B | THR374 |
| B | SER375 |
| B | 5GP506 |
| B | MG507 |
| B | HOH508 |
| B | HOH509 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 5GP B 506 |
| Chain | Residue |
| A | VAL325 |
| A | LYS326 |
| A | ARG328 |
| B | HIS25 |
| B | TYR258 |
| B | ALA260 |
| B | ARG261 |
| B | PRO262 |
| B | ARG275 |
| B | PRO302 |
| B | GLU303 |
| B | THR304 |
| B | LYS326 |
| B | 5GP505 |
| B | HOH508 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 5GP C 505 |
| Chain | Residue |
| C | ARG371 |
| C | GLY372 |
| C | THR373 |
| C | THR374 |
| C | 5GP506 |
| C | MG507 |
| C | HOH508 |
| C | HOH509 |
| C | TYR74 |
| C | PHE254 |
| C | TYR258 |
| C | ASP366 |
| C | ASP367 |
| C | SER368 |
| C | VAL370 |
| site_id | BC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 5GP C 506 |
| Chain | Residue |
| C | HIS25 |
| C | TYR258 |
| C | ALA260 |
| C | ARG261 |
| C | PRO262 |
| C | ARG275 |
| C | PRO302 |
| C | GLU303 |
| C | THR304 |
| C | LYS326 |
| C | 5GP505 |
| C | HOH508 |
| C | HOH520 |
| D | VAL325 |
| D | LYS326 |
| D | ARG328 |
| site_id | BC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 5GP D 505 |
| Chain | Residue |
| D | TYR74 |
| D | PHE254 |
| D | TYR258 |
| D | ASP366 |
| D | ASP367 |
| D | SER368 |
| D | VAL370 |
| D | ARG371 |
| D | GLY372 |
| D | THR373 |
| D | THR374 |
| D | 5GP506 |
| D | MG507 |
| D | HOH508 |
| D | HOH509 |
| site_id | BC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 5GP D 506 |
| Chain | Residue |
| C | VAL325 |
| C | LYS326 |
| C | ARG328 |
| D | HIS25 |
| D | TYR258 |
| D | ALA260 |
| D | ARG261 |
| D | PRO262 |
| D | ARG275 |
| D | PRO302 |
| D | GLU303 |
| D | THR304 |
| D | LYS326 |
| D | ASP367 |
| D | 5GP505 |
| D | HOH508 |
| D | HOH510 |
| 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 GMP IN THE CATALYTIC SITE. A SECOND PHOSPHATE GROUP, FROM THE PROXIMAL ALLOSTERIC REGULATORY SITE, OCCUPIES THE PYROPHOSPHATE BINDING REGION OF THE PRTASE ACTIVE SITE. ASP 366 AND ASP 367 FUNCTION AS METAL LIGANDS IN THE INHIBITED STATE OF THIS ENZYME, AND ARE THE HALLMARK OF PRTASE ENZYMES. MG++ IS PRESENT IN THIS STRUCTURE, AND IS LIGANDED TO ASP 366, ASP 367, THE TWO FURANOSE HYDROXYLS OF GMP, AND TWO WATERS. |
| 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 GMP IN THE CATALYTIC SITE. A SECOND PHOSPHATE GROUP, FROM THE PROXIMAL ALLOSTERIC REGULATORY SITE, OCCUPIES THE PYROPHOSPHATE BINDING REGION OF THE PRTASE ACTIVE SITE. ASP 366 AND ASP 367 FUNCTION AS METAL LIGANDS IN THE INHIBITED STATE OF THIS ENZYME, AND ARE THE HALLMARK OF PRTASE ENZYMES. MG++ IS PRESENT IN THIS STRUCTURE, AND IS LIGANDED TO ASP 366, ASP 367, THE TWO FURANOSE HYDROXYLS OF GMP, AND TWO WATERS. |
| 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 GMP IN THE CATALYTIC SITE. A SECOND PHOSPHATE GROUP, FROM THE PROXIMAL ALLOSTERIC REGULATORY SITE, OCCUPIES THE PYROPHOSPHATE BINDING REGION OF THE PRTASE ACTIVE SITE. ASP 366 AND ASP 367 FUNCTION AS METAL LIGANDS IN THE INHIBITED STATE OF THIS ENZYME, AND ARE THE HALLMARK OF PRTASE ENZYMES. MG++ IS PRESENT IN THIS STRUCTURE, AND IS LIGANDED TO ASP 366, ASP 367, THE TWO FURANOSE HYDROXYLS OF GMP, AND TWO WATERS. |
| 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 GMP IN THE CATALYTIC SITE. A SECOND PHOSPHATE GROUP, FROM THE PROXIMAL ALLOSTERIC REGULATORY SITE, OCCUPIES THE PYROPHOSPHATE BINDING REGION OF THE PRTASE ACTIVE SITE. ASP 366 AND ASP 367 FUNCTION AS METAL LIGANDS IN THE INHIBITED STATE OF THIS ENZYME, AND ARE THE HALLMARK OF PRTASE ENZYMES. MG++ IS PRESENT IN THIS STRUCTURE, AND IS LIGANDED TO ASP 366, ASP 367, THE TWO FURANOSE HYDROXYLS OF GMP, AND TWO WATERS. |
| 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 | 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 |
