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 | 0009113 | biological_process | purine nucleobase biosynthetic process |
| A | 0051536 | molecular_function | iron-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 | 0009113 | biological_process | purine nucleobase biosynthetic process |
| B | 0051536 | molecular_function | iron-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 | 0009113 | biological_process | purine nucleobase biosynthetic process |
| C | 0051536 | molecular_function | iron-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 | 0009113 | biological_process | purine nucleobase biosynthetic process |
| D | 0051536 | molecular_function | iron-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 | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01931","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"6411716","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01931","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8197456","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9271502","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01931","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9271502","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 |
