1P4R
Crystal Structure of Human ATIC in complex with folate-based inhibitor BW1540U88UD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003360 | biological_process | brainstem development |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003937 | molecular_function | IMP cyclohydrolase activity |
| A | 0004643 | molecular_function | phosphoribosylaminoimidazolecarboxamide formyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006177 | biological_process | GMP biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0008152 | biological_process | metabolic process |
| A | 0010035 | biological_process | response to inorganic substance |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0021549 | biological_process | cerebellum development |
| A | 0021987 | biological_process | cerebral cortex development |
| A | 0031100 | biological_process | animal organ regeneration |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| A | 0045296 | molecular_function | cadherin binding |
| A | 0046452 | biological_process | dihydrofolate metabolic process |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0097294 | biological_process | 'de novo' XMP biosynthetic process |
| A | 0098761 | biological_process | cellular response to interleukin-7 |
| B | 0003360 | biological_process | brainstem development |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003937 | molecular_function | IMP cyclohydrolase activity |
| B | 0004643 | molecular_function | phosphoribosylaminoimidazolecarboxamide formyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006177 | biological_process | GMP biosynthetic process |
| B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| B | 0008152 | biological_process | metabolic process |
| B | 0010035 | biological_process | response to inorganic substance |
| B | 0016020 | cellular_component | membrane |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0021549 | biological_process | cerebellum development |
| B | 0021987 | biological_process | cerebral cortex development |
| B | 0031100 | biological_process | animal organ regeneration |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| B | 0045296 | molecular_function | cadherin binding |
| B | 0046452 | biological_process | dihydrofolate metabolic process |
| B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0097294 | biological_process | 'de novo' XMP biosynthetic process |
| B | 0098761 | biological_process | cellular response to interleukin-7 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K A 1001 |
| Chain | Residue |
| A | VAL425 |
| A | THR428 |
| A | SER430 |
| A | SER432 |
| A | ASP539 |
| A | LEU589 |
| A | HIS591 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K B 1002 |
| Chain | Residue |
| B | SER430 |
| B | SER432 |
| B | ASP539 |
| B | LEU589 |
| B | HIS591 |
| B | VAL425 |
| B | THR428 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE AMZ A 1701 |
| Chain | Residue |
| A | ASN431 |
| A | ARG451 |
| A | ALA540 |
| A | PHE541 |
| A | ARG588 |
| A | PHE590 |
| A | 3541801 |
| A | HOH1911 |
| A | HOH1930 |
| B | ARG207 |
| B | TYR208 |
| B | ASN239 |
| B | LYS266 |
| B | HIS267 |
| B | GLY316 |
| B | ASP339 |
| B | HOH1805 |
| B | HOH1818 |
| B | HOH1838 |
| B | HOH1938 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE AMZ B 1702 |
| Chain | Residue |
| A | ARG207 |
| A | TYR208 |
| A | LYS266 |
| A | HIS267 |
| A | GLY316 |
| A | ASP339 |
| A | HOH1903 |
| A | HOH1908 |
| A | HOH1931 |
| B | ASN431 |
| B | ARG451 |
| B | ALA540 |
| B | PHE541 |
| B | ARG588 |
| B | PHE590 |
| B | 3541802 |
| B | HOH1855 |
| B | HOH1859 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE 354 A 1801 |
| Chain | Residue |
| A | ASN431 |
| A | GLN449 |
| A | SER450 |
| A | ARG451 |
| A | ILE452 |
| A | PHE541 |
| A | PRO543 |
| A | PHE544 |
| A | ASP546 |
| A | ASN547 |
| A | SER565 |
| A | ALA566 |
| A | AMZ1701 |
| A | HOH1947 |
| A | HOH1952 |
| A | HOH1962 |
| B | LYS266 |
| B | MET312 |
| B | PHE315 |
| B | GLY316 |
| B | ASN489 |
| B | HOH1815 |
| site_id | AC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE 354 B 1802 |
| Chain | Residue |
| A | LYS266 |
| A | MET312 |
| A | PHE315 |
| A | ASN489 |
| B | ASN431 |
| B | GLN449 |
| B | SER450 |
| B | ARG451 |
| B | ILE452 |
| B | PHE541 |
| B | PRO543 |
| B | PHE544 |
| B | ASP546 |
| B | ASN547 |
| B | SER565 |
| B | ALA566 |
| B | AMZ1702 |
| B | HOH1856 |
| B | HOH1858 |
| B | HOH1932 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE XMP A 1901 |
| Chain | Residue |
| A | GLY36 |
| A | THR37 |
| A | ARG64 |
| A | LYS66 |
| A | THR67 |
| A | LEU68 |
| A | CYS101 |
| A | ASN102 |
| A | LEU103 |
| A | TYR104 |
| A | ASP125 |
| A | ILE126 |
| A | GLY127 |
| A | GLY128 |
| A | SER10 |
| A | VAL11 |
| A | SER12 |
| A | LYS14 |
| A | SER34 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor; for FAICAR cyclization activity => ECO:0000305|PubMed:14756553 |
| Chain | Residue | Details |
| A | LYS137 | |
| B | LYS137 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor; for AICAR formyltransferase activity => ECO:0000305|PubMed:14966129 |
| Chain | Residue | Details |
| A | HIS267 | |
| B | HIS267 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:14756553, ECO:0000305|PubMed:14966129, ECO:0007744|PDB:1P4R, ECO:0007744|PDB:1PKX, ECO:0007744|PDB:1PL0 |
| Chain | Residue | Details |
| A | SER12 | |
| B | ASP125 | |
| A | SER34 | |
| A | ARG64 | |
| A | CYS101 | |
| A | ASP125 | |
| B | SER12 | |
| B | SER34 | |
| B | ARG64 | |
| B | CYS101 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:14966129, ECO:0007744|PDB:1P4R, ECO:0007744|PDB:1PL0 |
| Chain | Residue | Details |
| A | ARG207 | |
| B | ARG207 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:14966129, ECO:0000269|PubMed:29072452, ECO:0007744|PDB:1P4R, ECO:0007744|PDB:1PL0 |
| Chain | Residue | Details |
| A | HIS267 | |
| A | GLY316 | |
| A | ASP339 | |
| B | HIS267 | |
| B | GLY316 | |
| B | ASP339 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14966129, ECO:0000269|PubMed:29072452, ECO:0007744|PDB:1P4R, ECO:0007744|PDB:1PL0 |
| Chain | Residue | Details |
| A | ASN431 | |
| A | ARG451 | |
| A | PHE541 | |
| A | ARG588 | |
| B | ASN431 | |
| B | ARG451 | |
| B | PHE541 | |
| B | ARG588 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P31335 |
| Chain | Residue | Details |
| A | ILE452 | |
| A | ASP546 | |
| A | SER565 | |
| B | ILE452 | |
| B | ASP546 | |
| B | SER565 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:14966129 |
| Chain | Residue | Details |
| A | LYS266 | |
| B | LYS266 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330 |
| Chain | Residue | Details |
| A | MET1 | |
| B | MET1 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS199 | |
| B | LYS199 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 646 |
| Chain | Residue | Details |
| A | LYS266 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| A | HIS267 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| A | ASN431 | electrostatic stabiliser, modifies pKa |
| A | HIS592 | electrostatic stabiliser, modifies pKa, proton acceptor, proton donor, proton relay |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 646 |
| Chain | Residue | Details |
| B | LYS266 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| B | HIS267 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| B | ASN431 | electrostatic stabiliser, modifies pKa |
| B | HIS592 | electrostatic stabiliser, modifies pKa, proton acceptor, proton donor, proton relay |
