1GPH
STRUCTURE OF THE ALLOSTERIC REGULATORY ENZYME OF PURINE BIOSYNTHESIS
Functional Information from GO Data
Chain | GOid | namespace | contents |
1 | 0000287 | molecular_function | magnesium ion binding |
1 | 0004044 | molecular_function | amidophosphoribosyltransferase activity |
1 | 0006164 | biological_process | purine nucleotide biosynthetic process |
1 | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
1 | 0006541 | biological_process | glutamine metabolic process |
1 | 0009113 | biological_process | purine nucleobase biosynthetic process |
1 | 0016757 | molecular_function | glycosyltransferase activity |
1 | 0046872 | molecular_function | metal ion binding |
1 | 0051536 | molecular_function | iron-sulfur cluster binding |
1 | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
2 | 0000287 | molecular_function | magnesium ion binding |
2 | 0004044 | molecular_function | amidophosphoribosyltransferase activity |
2 | 0006164 | biological_process | purine nucleotide biosynthetic process |
2 | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
2 | 0006541 | biological_process | glutamine metabolic process |
2 | 0009113 | biological_process | purine nucleobase biosynthetic process |
2 | 0016757 | molecular_function | glycosyltransferase activity |
2 | 0046872 | molecular_function | metal ion binding |
2 | 0051536 | molecular_function | iron-sulfur cluster binding |
2 | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
3 | 0000287 | molecular_function | magnesium ion binding |
3 | 0004044 | molecular_function | amidophosphoribosyltransferase activity |
3 | 0006164 | biological_process | purine nucleotide biosynthetic process |
3 | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
3 | 0006541 | biological_process | glutamine metabolic process |
3 | 0009113 | biological_process | purine nucleobase biosynthetic process |
3 | 0016757 | molecular_function | glycosyltransferase activity |
3 | 0046872 | molecular_function | metal ion binding |
3 | 0051536 | molecular_function | iron-sulfur cluster binding |
3 | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
4 | 0000287 | molecular_function | magnesium ion binding |
4 | 0004044 | molecular_function | amidophosphoribosyltransferase activity |
4 | 0006164 | biological_process | purine nucleotide biosynthetic process |
4 | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
4 | 0006541 | biological_process | glutamine metabolic process |
4 | 0009113 | biological_process | purine nucleobase biosynthetic process |
4 | 0016757 | molecular_function | glycosyltransferase activity |
4 | 0046872 | molecular_function | metal ion binding |
4 | 0051536 | molecular_function | iron-sulfur cluster binding |
4 | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
site_id | A11 |
Number of Residues | 10 |
Details |
Chain | Residue |
1 | ASP345 |
1 | ASP346 |
1 | SER347 |
1 | ILE348 |
1 | VAL349 |
1 | ARG350 |
1 | GLY351 |
1 | THR352 |
1 | THR353 |
1 | AMP467 |
site_id | A12 |
Number of Residues | 11 |
Details |
Chain | Residue |
1 | TYR242 |
1 | PHE243 |
1 | SER244 |
1 | ARG245 |
1 | PRO246 |
1 | ASP247 |
1 | LYS305 |
1 | AMP468 |
2 | LYS305 |
2 | ASN306 |
2 | ARG307 |
site_id | A21 |
Number of Residues | 10 |
Details |
Chain | Residue |
2 | ASP345 |
2 | ASP346 |
2 | SER347 |
2 | ILE348 |
2 | VAL349 |
2 | ARG350 |
2 | GLY351 |
2 | THR352 |
2 | THR353 |
2 | AMP467 |
site_id | A22 |
Number of Residues | 11 |
Details |
Chain | Residue |
2 | TYR242 |
2 | PHE243 |
2 | SER244 |
2 | ARG245 |
2 | PRO246 |
2 | ASP247 |
2 | LYS305 |
2 | AMP468 |
1 | LYS305 |
1 | ASN306 |
1 | ARG307 |
site_id | A31 |
Number of Residues | 10 |
Details |
Chain | Residue |
3 | ASP345 |
3 | ASP346 |
3 | SER347 |
3 | ILE348 |
3 | VAL349 |
3 | ARG350 |
3 | GLY351 |
3 | THR352 |
3 | THR353 |
3 | AMP467 |
site_id | A32 |
Number of Residues | 11 |
Details |
Chain | Residue |
3 | TYR242 |
3 | PHE243 |
3 | SER244 |
3 | ARG245 |
3 | PRO246 |
3 | ASP247 |
3 | LYS305 |
3 | AMP468 |
4 | LYS305 |
4 | ASN306 |
4 | ARG307 |
site_id | A41 |
Number of Residues | 10 |
Details |
Chain | Residue |
4 | ASP345 |
4 | ASP346 |
4 | SER347 |
4 | ILE348 |
4 | VAL349 |
4 | ARG350 |
4 | GLY351 |
4 | THR352 |
4 | THR353 |
4 | AMP467 |
site_id | A42 |
Number of Residues | 11 |
Details |
Chain | Residue |
4 | LYS305 |
4 | AMP468 |
3 | LYS305 |
3 | ASN306 |
3 | ARG307 |
4 | TYR242 |
4 | PHE243 |
4 | SER244 |
4 | ARG245 |
4 | PRO246 |
4 | ASP247 |
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 1 466 |
Chain | Residue |
1 | CYS236 |
1 | SER237 |
1 | CYS382 |
1 | TYR384 |
1 | THR388 |
1 | CYS437 |
1 | ALA439 |
1 | CYS440 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE AMP 1 467 |
Chain | Residue |
1 | TYR242 |
1 | SER283 |
1 | ASP345 |
1 | ASP346 |
1 | SER347 |
1 | VAL349 |
1 | ARG350 |
1 | GLY351 |
1 | THR352 |
1 | THR353 |
1 | THR388 |
1 | SER389 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE AMP 1 468 |
Chain | Residue |
1 | TYR242 |
1 | SER244 |
1 | ARG245 |
1 | PRO246 |
1 | ARG259 |
1 | PRO281 |
1 | ASP282 |
1 | SER283 |
1 | LYS305 |
2 | ILE304 |
2 | LYS305 |
2 | ARG307 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SF4 2 466 |
Chain | Residue |
2 | CYS236 |
2 | SER237 |
2 | CYS382 |
2 | TYR384 |
2 | THR388 |
2 | CYS437 |
2 | CYS440 |
site_id | AC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE AMP 2 467 |
Chain | Residue |
2 | TYR73 |
2 | TYR242 |
2 | SER283 |
2 | ASP345 |
2 | ASP346 |
2 | SER347 |
2 | VAL349 |
2 | ARG350 |
2 | GLY351 |
2 | THR352 |
2 | THR353 |
2 | ASP387 |
site_id | AC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE AMP 2 468 |
Chain | Residue |
1 | ILE304 |
1 | LYS305 |
1 | ARG307 |
2 | TYR242 |
2 | SER244 |
2 | ARG245 |
2 | ARG259 |
2 | PRO281 |
2 | ASP282 |
2 | SER283 |
2 | LYS305 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 3 466 |
Chain | Residue |
3 | CYS236 |
3 | SER237 |
3 | MET238 |
3 | CYS382 |
3 | TYR384 |
3 | THR388 |
3 | CYS437 |
3 | ALA439 |
3 | CYS440 |
site_id | AC8 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE AMP 3 467 |
Chain | Residue |
3 | MET238 |
3 | TYR242 |
3 | SER283 |
3 | ASP345 |
3 | ASP346 |
3 | SER347 |
3 | VAL349 |
3 | ARG350 |
3 | GLY351 |
3 | THR352 |
3 | THR353 |
3 | THR388 |
3 | SER389 |
3 | AMP468 |
site_id | AC9 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE AMP 3 468 |
Chain | Residue |
3 | TYR242 |
3 | SER244 |
3 | ARG245 |
3 | PRO246 |
3 | ARG259 |
3 | PRO281 |
3 | ASP282 |
3 | SER283 |
3 | LYS305 |
3 | AMP467 |
4 | LYS305 |
4 | ARG307 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 4 466 |
Chain | Residue |
4 | CYS236 |
4 | SER237 |
4 | MET238 |
4 | CYS382 |
4 | TYR384 |
4 | THR388 |
4 | CYS437 |
4 | CYS440 |
site_id | BC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE AMP 4 467 |
Chain | Residue |
4 | TYR242 |
4 | SER283 |
4 | ASP345 |
4 | ASP346 |
4 | SER347 |
4 | VAL349 |
4 | ARG350 |
4 | GLY351 |
4 | THR352 |
4 | THR353 |
4 | ASP387 |
4 | THR388 |
4 | SER389 |
site_id | BC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE AMP 4 468 |
Chain | Residue |
3 | ILE304 |
3 | LYS305 |
3 | ARG307 |
4 | TYR242 |
4 | SER244 |
4 | ARG245 |
4 | PRO246 |
4 | ARG259 |
4 | PRO281 |
4 | ASP282 |
4 | SER283 |
4 | LYS305 |
site_id | FS1 |
Number of Residues | 5 |
Details |
Chain | Residue |
1 | SF4466 |
1 | CYS236 |
1 | CYS382 |
1 | CYS437 |
1 | CYS440 |
site_id | FS2 |
Number of Residues | 5 |
Details |
Chain | Residue |
2 | CYS440 |
2 | SF4466 |
2 | CYS236 |
2 | CYS382 |
2 | CYS437 |
site_id | FS3 |
Number of Residues | 5 |
Details |
Chain | Residue |
3 | SF4466 |
3 | CYS236 |
3 | CYS382 |
3 | CYS437 |
3 | CYS440 |
site_id | FS4 |
Number of Residues | 5 |
Details |
Chain | Residue |
4 | SF4466 |
4 | CYS236 |
4 | CYS382 |
4 | CYS437 |
4 | CYS440 |
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 |
1 | 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 |
1 | CYS1 | |
2 | CYS1 | |
3 | CYS1 | |
4 | 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 |
1 | CYS236 | |
3 | CYS382 | |
3 | CYS437 | |
3 | CYS440 | |
4 | CYS236 | |
4 | CYS382 | |
4 | CYS437 | |
4 | CYS440 | |
1 | CYS382 | |
1 | CYS437 | |
1 | CYS440 | |
2 | CYS236 | |
2 | CYS382 | |
2 | CYS437 | |
2 | CYS440 | |
3 | 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 |
1 | SER283 | |
4 | SER283 | |
4 | ASP345 | |
4 | ASP346 | |
1 | ASP345 | |
1 | ASP346 | |
2 | SER283 | |
2 | ASP345 | |
2 | ASP346 | |
3 | SER283 | |
3 | ASP345 | |
3 | ASP346 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
1 | ASP345 | |
1 | LYS372 | |
1 | VAL349 | |
1 | ASP346 |
site_id | CSA10 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
2 | GLY324 |
site_id | CSA11 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
3 | GLY324 |
site_id | CSA12 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
4 | GLY324 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
2 | ASP345 | |
2 | LYS372 | |
2 | VAL349 | |
2 | ASP346 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
3 | ASP345 | |
3 | LYS372 | |
3 | VAL349 | |
3 | ASP346 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
4 | ASP345 | |
4 | LYS372 | |
4 | VAL349 | |
4 | ASP346 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
1 | GLY103 | |
1 | ASN102 | |
1 | CYS1 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
2 | GLY103 | |
2 | ASN102 | |
2 | CYS1 |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
3 | GLY103 | |
3 | ASN102 | |
3 | CYS1 |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
4 | GLY103 | |
4 | ASN102 | |
4 | CYS1 |
site_id | CSA9 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
1 | GLY324 |