1ECF
ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE
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 | 0016740 | molecular_function | transferase activity |
| 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 | 0016740 | molecular_function | transferase activity |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PIN A 505 |
| Chain | Residue |
| A | PRO302 |
| A | GLU303 |
| A | THR304 |
| A | ASP366 |
| A | ASP367 |
| A | SER368 |
| A | VAL370 |
| A | ARG371 |
| A | GLY372 |
| A | THR373 |
| A | THR374 |
| A | HOH551 |
| A | HOH849 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PIN A 506 |
| Chain | Residue |
| A | ARG43 |
| A | LEU44 |
| A | ARG45 |
| A | LYS46 |
| A | ARG62 |
| A | HOH810 |
| A | HOH836 |
| A | HOH836 |
| A | HOH982 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PIN A 507 |
| Chain | Residue |
| A | TYR89 |
| A | TYR89 |
| A | VAL90 |
| A | VAL90 |
| A | ASN91 |
| A | ASN91 |
| A | HOH511 |
| A | HOH511 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PIN B 505 |
| Chain | Residue |
| A | HOH786 |
| B | GLU303 |
| B | THR304 |
| B | LYS326 |
| B | ASP366 |
| B | ASP367 |
| B | SER368 |
| B | ILE369 |
| B | VAL370 |
| B | ARG371 |
| B | GLY372 |
| B | THR373 |
| B | THR374 |
| B | SER375 |
| B | HOH848 |
| B | HOH910 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PIN B 506 |
| Chain | Residue |
| B | ARG43 |
| B | LEU44 |
| B | LEU44 |
| B | ARG45 |
| B | LYS46 |
| B | ARG62 |
| B | ARG62 |
| B | GLU84 |
| B | HOH770 |
| B | HOH884 |
| B | HOH943 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PIN B 507 |
| Chain | Residue |
| B | TYR89 |
| B | TYR89 |
| B | VAL90 |
| B | VAL90 |
| B | ASN91 |
| B | ASN91 |
| B | SER92 |
| B | HOH555 |
| site_id | NTA |
| Number of Residues | 1 |
| Details | NTN TYPE GLUTAMINE AMIDOTRANSFERASE CATALYTIC RESIDUE. THIS SITE BELONGS TO THE NTN SUPERFAMILY, WHICH ARE THOUGHT TO UTILIZE THE ALPHA-AMINO GROUP OF THE N-TERMINAL RESIDUE AS A PROTON DONOR , AND THE SIDE CHAIN OF THIS RESIDUE AS A NUCLEOPHILE IN CATALYSIS OF A HYDROLYTIC REACTION. |
| Chain | Residue |
| A | CYS1 |
| site_id | NTB |
| Number of Residues | 1 |
| Details | NTN TYPE GLUTAMINE AMIDOTRANSFERASE CATALYTIC RESIDUE. THIS SITE BELONGS TO THE NTN SUPERFAMILY, WHICH ARE THOUGHT TO UTILIZE THE ALPHA-AMINO GROUP OF THE N-TERMINAL RESIDUE AS A PROTON DONOR , AND THE SIDE CHAIN OF THIS RESIDUE AS A NUCLEOPHILE IN CATALYSIS OF A HYDROLYTIC REACTION. |
| Chain | Residue |
| B | CYS1 |
| site_id | PRA |
| Number of Residues | 13 |
| Details | PRPP BINDING MOTIF, IDENTIFIED BY SEQUENCE SIMILARITY AMONG MEMBERS OF THE PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES. |
| Chain | Residue |
| A | ILE369 |
| A | VAL370 |
| A | ARG371 |
| A | GLY372 |
| A | THR373 |
| A | THR374 |
| A | VAL362 |
| A | LEU363 |
| A | LEU364 |
| A | VAL365 |
| A | ASP366 |
| A | ASP367 |
| A | SER368 |
| site_id | PRB |
| Number of Residues | 13 |
| Details | PRPP BINDING MOTIF, IDENTIFIED BY SEQUENCE SIMILARITY AMONG MEMBERS OF THE PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES. |
| Chain | Residue |
| B | VAL362 |
| B | LEU363 |
| B | LEU364 |
| B | VAL365 |
| B | ASP366 |
| B | ASP367 |
| B | SER368 |
| B | ILE369 |
| B | VAL370 |
| B | ARG371 |
| B | GLY372 |
| B | THR373 |
| B | THR374 |
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 | 468 |
| Details | Domain: {"description":"Glutamine amidotransferase type-2","evidences":[{"source":"HAMAP-Rule","id":"MF_01931","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01931","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7037784","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01931","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9514258, 9914248 |
| Chain | Residue | Details |
| A | CYS1 | |
| A | ASN101 | |
| A | GLY102 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 214 |
| Chain | Residue | Details |
| A | CYS1 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | GLY27 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | ASN101 | electrostatic stabiliser, hydrogen bond donor |
| A | GLY102 | electrostatic stabiliser, hydrogen bond donor |
| A | TYR258 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 214 |
| Chain | Residue | Details |
| B | CYS1 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | GLY27 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| B | ASN101 | electrostatic stabiliser, hydrogen bond donor |
| B | GLY102 | electrostatic stabiliser, hydrogen bond donor |
| B | TYR258 | electrostatic stabiliser, hydrogen bond donor |
