1AO0
GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE FROM B. SUBTILIS COMPLEXED WITH ADP AND GMP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004044 | molecular_function | amidophosphoribosyltransferase activity |
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 | 0046872 | molecular_function | metal ion binding |
A | 0051536 | molecular_function | iron-sulfur cluster binding |
A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004044 | molecular_function | amidophosphoribosyltransferase activity |
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 | 0046872 | molecular_function | metal ion binding |
B | 0051536 | molecular_function | iron-sulfur cluster binding |
B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0004044 | molecular_function | amidophosphoribosyltransferase activity |
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 | 0046872 | molecular_function | metal ion binding |
C | 0051536 | molecular_function | iron-sulfur cluster binding |
C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0004044 | molecular_function | amidophosphoribosyltransferase activity |
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 | 0046872 | molecular_function | metal ion binding |
D | 0051536 | molecular_function | iron-sulfur cluster binding |
D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 469 |
Chain | Residue |
A | SER283 |
A | ASP345 |
A | ASP346 |
A | 5GP467 |
A | HOH470 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 469 |
Chain | Residue |
B | SER283 |
B | ASP345 |
B | ASP346 |
B | 5GP467 |
B | HOH470 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 469 |
Chain | Residue |
C | SER283 |
C | ASP345 |
C | ASP346 |
C | 5GP467 |
C | HOH470 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 469 |
Chain | Residue |
D | SER283 |
D | ASP345 |
D | ASP346 |
D | 5GP467 |
D | HOH470 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SF4 A 466 |
Chain | Residue |
A | CYS236 |
A | SER237 |
A | MET238 |
A | CYS382 |
A | CYS437 |
A | ALA439 |
A | CYS440 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 5GP A 467 |
Chain | Residue |
A | MET238 |
A | TYR242 |
A | SER283 |
A | ASP345 |
A | ASP346 |
A | SER347 |
A | VAL349 |
A | ARG350 |
A | GLY351 |
A | THR352 |
A | THR353 |
A | ASP387 |
A | ADP468 |
A | MG469 |
A | HOH470 |
site_id | AC7 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ADP A 468 |
Chain | Residue |
A | HIS25 |
A | TYR242 |
A | SER244 |
A | ARG245 |
A | PRO246 |
A | ARG259 |
A | PRO281 |
A | ASP282 |
A | SER283 |
A | LYS305 |
A | 5GP467 |
B | ILE304 |
B | LYS305 |
B | ARG307 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SF4 B 466 |
Chain | Residue |
B | CYS236 |
B | SER237 |
B | MET238 |
B | CYS382 |
B | CYS437 |
B | ALA439 |
B | CYS440 |
site_id | AC9 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 5GP B 467 |
Chain | Residue |
B | MET238 |
B | TYR242 |
B | SER283 |
B | ASP345 |
B | ASP346 |
B | SER347 |
B | VAL349 |
B | ARG350 |
B | GLY351 |
B | THR352 |
B | THR353 |
B | ASP387 |
B | ADP468 |
B | MG469 |
B | HOH470 |
site_id | AMA |
Number of Residues | 1 |
Details | ALLOSTERIC NUCLEOTIDE BINDING SITE AT INTERFACE OF A AND B MONOMERS, NEAR MOLECULAR TWO-FOLD AXIS, IDENTIFIED BY BINDING OF ADP. |
Chain | Residue |
A | ADP468 |
site_id | AMB |
Number of Residues | 1 |
Details | ALLOSTERIC NUCLEOTIDE BINDING SITE AT INTERFACE OF A AND B MONOMERS, NEAR MOLECULAR TWO-FOLD AXIS, IDENTIFIED BY BINDING OF ADP. |
Chain | Residue |
B | ADP468 |
site_id | AMC |
Number of Residues | 1 |
Details | ALLOSTERIC NUCLEOTIDE BINDING SITE AT INTERFACE OF C AND D MONOMERS, NEAR MOLECULAR TWO-FOLD AXIS, IDENTIFIED BY BINDING OF ADP. |
Chain | Residue |
C | ADP468 |
site_id | AMD |
Number of Residues | 1 |
Details | ALLOSTERIC NUCLEOTIDE BINDING SITE AT INTERFACE OF C AND D MONOMERS, NEAR MOLECULAR TWO-FOLD AXIS, IDENTIFIED BY BINDING OF ADP. |
Chain | Residue |
D | ADP468 |
site_id | BC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ADP B 468 |
Chain | Residue |
B | ARG245 |
B | PRO246 |
B | ARG259 |
B | PRO281 |
B | ASP282 |
B | SER283 |
B | LYS305 |
B | 5GP467 |
A | ILE304 |
A | LYS305 |
A | ARG307 |
B | TYR242 |
B | SER244 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 C 466 |
Chain | Residue |
C | CYS236 |
C | SER237 |
C | MET238 |
C | CYS382 |
C | TYR384 |
C | CYS437 |
C | ALA439 |
C | CYS440 |
site_id | BC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 5GP C 467 |
Chain | Residue |
C | MET238 |
C | TYR242 |
C | SER283 |
C | ASP345 |
C | ASP346 |
C | SER347 |
C | VAL349 |
C | ARG350 |
C | GLY351 |
C | THR352 |
C | THR353 |
C | ASP387 |
C | ADP468 |
C | MG469 |
C | HOH470 |
site_id | BC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ADP C 468 |
Chain | Residue |
C | TYR242 |
C | SER244 |
C | ARG245 |
C | PRO246 |
C | ARG259 |
C | PRO281 |
C | ASP282 |
C | SER283 |
C | LYS305 |
C | 5GP467 |
D | ILE304 |
D | LYS305 |
D | ARG307 |
site_id | BC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 D 466 |
Chain | Residue |
D | CYS236 |
D | SER237 |
D | MET238 |
D | CYS382 |
D | TYR384 |
D | CYS437 |
D | ALA439 |
D | CYS440 |
site_id | BC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 5GP D 467 |
Chain | Residue |
D | MET238 |
D | TYR242 |
D | SER283 |
D | ASP345 |
D | ASP346 |
D | SER347 |
D | VAL349 |
D | ARG350 |
D | GLY351 |
D | THR352 |
D | THR353 |
D | ASP387 |
D | ADP468 |
D | MG469 |
D | HOH470 |
site_id | BC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ADP D 468 |
Chain | Residue |
C | ILE304 |
C | LYS305 |
C | ARG307 |
D | TYR242 |
D | SER244 |
D | ARG245 |
D | PRO246 |
D | ARG259 |
D | PRO281 |
D | ASP282 |
D | SER283 |
D | LYS305 |
D | 5GP467 |
site_id | MGA |
Number of Residues | 1 |
Details | MG2+ ION BINDING SITE. THE MG2+ ION IS OCTAHEDRALLY COORDINATED BY THE OXYGENS OF THREE AMINO ACID SIDE CHAINS, THE TWO RIBOSE HYDROXYL OXYGENS OF THE GMP INHIBITOR, AND A WATER. |
Chain | Residue |
A | MG469 |
site_id | MGB |
Number of Residues | 1 |
Details | MG2+ ION BINDING SITE. THE MG2+ ION IS OCTAHEDRALLY COORDINATED BY THE OXYGENS OF THREE AMINO ACID SIDE CHAINS, THE TWO RIBOSE HYDROXYL OXYGENS OF THE GMP INHIBITOR, AND A WATER. |
Chain | Residue |
B | MG469 |
site_id | MGC |
Number of Residues | 1 |
Details | MG2+ ION BINDING SITE. THE MG2+ ION IS OCTAHEDRALLY COORDINATED BY THE OXYGENS OF THREE AMINO ACID SIDE CHAINS, THE TWO RIBOSE HYDROXYL OXYGENS OF THE GMP INHIBITOR, AND A WATER. |
Chain | Residue |
C | MG469 |
site_id | MGD |
Number of Residues | 1 |
Details | MG2+ ION BINDING SITE. THE MG2+ ION IS OCTAHEDRALLY COORDINATED BY THE OXYGENS OF THREE AMINO ACID SIDE CHAINS, THE TWO RIBOSE HYDROXYL OXYGENS OF THE GMP INHIBITOR, AND A WATER. |
Chain | Residue |
D | MG469 |
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 | NTC |
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 |
C | CYS1 |
site_id | NTD |
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 |
D | CYS1 |
site_id | PRA |
Number of Residues | 1 |
Details | DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE)FAMILY OF ENZYMES, AND NUCLEOTIDE INHIBITOR (IN THIS CASE, 5GP) BINDING SITE. |
Chain | Residue |
A | 5GP467 |
site_id | PRB |
Number of Residues | 1 |
Details | DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE)FAMILY OF ENZYMES, AND NUCLEOTIDE INHIBITOR (IN THIS CASE, 5GP) BINDING SITE. |
Chain | Residue |
B | 5GP467 |
site_id | PRC |
Number of Residues | 1 |
Details | DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE)FAMILY OF ENZYMES, AND NUCLEOTIDE INHIBITOR (IN THIS CASE, 5GP) BINDING SITE. |
Chain | Residue |
C | 5GP467 |
site_id | PRD |
Number of Residues | 1 |
Details | DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE)FAMILY OF ENZYMES, AND NUCLEOTIDE INHIBITOR (IN THIS CASE, 5GP) BINDING SITE. |
Chain | Residue |
D | 5GP467 |
Functional Information from PROSITE/UniProt
site_id | PS00103 |
Number of Residues | 13 |
Details | PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VVMVDDSIVRGtT |
Chain | Residue | Details |
A | VAL341-THR353 |
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:6411716 |
Chain | Residue | Details |
A | CYS1 | |
B | CYS1 | |
C | CYS1 | |
D | CYS1 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000269|PubMed:8197456, ECO:0000269|PubMed:9271502 |
Chain | Residue | Details |
A | CYS236 | |
C | CYS382 | |
C | CYS437 | |
C | CYS440 | |
D | CYS236 | |
D | CYS382 | |
D | CYS437 | |
D | CYS440 | |
A | CYS382 | |
A | CYS437 | |
A | CYS440 | |
B | CYS236 | |
B | CYS382 | |
B | CYS437 | |
B | CYS440 | |
C | CYS236 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000269|PubMed:9271502 |
Chain | Residue | Details |
A | SER283 | |
D | SER283 | |
D | ASP345 | |
D | ASP346 | |
A | ASP345 | |
A | ASP346 | |
B | SER283 | |
B | ASP345 | |
B | ASP346 | |
C | SER283 | |
C | ASP345 | |
C | ASP346 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
A | ASP345 | |
A | LYS372 | |
A | VAL349 | |
A | ASP346 |
site_id | CSA10 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
B | GLY324 |
site_id | CSA11 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
C | GLY324 |
site_id | CSA12 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
D | GLY324 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
B | ASP345 | |
B | LYS372 | |
B | VAL349 | |
B | ASP346 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
C | ASP345 | |
C | LYS372 | |
C | VAL349 | |
C | ASP346 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
D | ASP345 | |
D | LYS372 | |
D | VAL349 | |
D | ASP346 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
A | GLY103 | |
A | ASN102 | |
A | CYS1 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
B | GLY103 | |
B | ASN102 | |
B | CYS1 |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
C | GLY103 | |
C | ASN102 | |
C | CYS1 |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
D | GLY103 | |
D | ASN102 | |
D | CYS1 |
site_id | CSA9 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
A | GLY324 |