1ECG
DON INACTIVATED 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 | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ONL A 505 |
| Chain | Residue |
| A | CYS1 |
| A | TYR74 |
| A | THR76 |
| A | SER79 |
| A | GLN86 |
| A | ASN101 |
| A | GLY102 |
| A | ASN103 |
| A | SER126 |
| A | ASP127 |
| A | SER128 |
| A | HOH532 |
| A | HOH1007 |
| A | HOH1008 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PIN A 506 |
| Chain | Residue |
| A | PRO302 |
| A | GLU303 |
| A | THR304 |
| A | ASP367 |
| A | SER368 |
| A | VAL370 |
| A | ARG371 |
| A | GLY372 |
| A | THR373 |
| A | THR374 |
| A | HOH551 |
| A | HOH842 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PIN A 507 |
| Chain | Residue |
| A | ARG43 |
| A | LEU44 |
| A | LEU44 |
| A | ARG45 |
| A | LYS46 |
| A | ARG62 |
| A | GLU84 |
| A | HOH804 |
| A | HOH829 |
| A | HOH829 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PIN A 508 |
| Chain | Residue |
| A | TYR89 |
| A | TYR89 |
| A | VAL90 |
| A | VAL90 |
| A | ASN91 |
| A | ASN91 |
| A | HOH512 |
| A | HOH512 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ONL B 505 |
| Chain | Residue |
| B | CYS1 |
| B | TYR74 |
| B | THR76 |
| B | SER79 |
| B | GLN86 |
| B | ASN101 |
| B | GLY102 |
| B | ASN103 |
| B | SER126 |
| B | ASP127 |
| B | SER128 |
| B | HOH774 |
| B | HOH986 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PIN B 506 |
| Chain | Residue |
| B | HOH850 |
| B | HOH917 |
| A | HOH780 |
| B | TYR258 |
| B | GLU303 |
| B | THR304 |
| B | ASP366 |
| B | ASP367 |
| B | SER368 |
| B | ILE369 |
| B | VAL370 |
| B | ARG371 |
| B | GLY372 |
| B | THR373 |
| B | THR374 |
| B | SER375 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PIN B 507 |
| Chain | Residue |
| B | ARG43 |
| B | LEU44 |
| B | LEU44 |
| B | ARG45 |
| B | LYS46 |
| B | ARG62 |
| B | ARG62 |
| B | GLU84 |
| B | HOH890 |
| B | HOH950 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PIN B 508 |
| Chain | Residue |
| B | TYR89 |
| B | TYR89 |
| B | VAL90 |
| B | VAL90 |
| B | ASN91 |
| B | ASN91 |
| B | HOH556 |
| B | HOH705 |
| 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 | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000269|PubMed:7037784 |
| Chain | Residue | Details |
| A | GLY2 | |
| B | GLY2 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01931 |
| Chain | Residue | Details |
| A | SER305 | |
| A | ASP367 | |
| A | SER368 | |
| B | SER305 | |
| B | ASP367 | |
| B | SER368 |
Catalytic Information from CSA
| 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 | 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 |
