1OZ0
CRYSTAL STRUCTURE OF THE HOMODIMERIC BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME AVIAN ATIC IN COMPLEX WITH A MULTISUBSTRATE ADDUCT INHIBITOR BETA-DADF.
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0006164 | biological_process | purine nucleotide biosynthetic process |
A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0042803 | molecular_function | protein homodimerization activity |
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 | 0006164 | biological_process | purine nucleotide biosynthetic process |
B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE K B 1003 |
Chain | Residue |
B | VAL426 |
B | THR429 |
B | SER431 |
B | SER433 |
B | ASP540 |
B | LEU590 |
B | HIS592 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE K A 1004 |
Chain | Residue |
A | SER431 |
A | SER433 |
A | ASP540 |
A | LEU590 |
A | HIS592 |
A | VAL426 |
A | THR429 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 1005 |
Chain | Residue |
A | SER11 |
A | SER35 |
A | GLY36 |
A | GLY37 |
A | THR38 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 B 1006 |
Chain | Residue |
B | SER11 |
B | LYS15 |
B | SER35 |
B | GLY36 |
B | GLY37 |
B | THR38 |
B | LYS67 |
site_id | AC5 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE MS1 B 1001 |
Chain | Residue |
A | ARG208 |
A | TYR209 |
A | ILE239 |
A | ASN240 |
A | LYS267 |
A | MET313 |
A | PHE316 |
A | GLY317 |
A | ASP340 |
A | HOH1034 |
A | HOH1063 |
B | GLN450 |
B | SER451 |
B | ARG452 |
B | ILE453 |
B | ALA541 |
B | PHE542 |
B | PRO544 |
B | PHE545 |
B | ASP547 |
B | SER566 |
B | ALA567 |
B | ARG589 |
B | PHE591 |
B | HOH1007 |
B | HOH1008 |
B | HOH1028 |
B | HOH1037 |
B | HOH1047 |
B | HOH1092 |
B | HOH1117 |
B | HOH1127 |
B | HOH1160 |
B | HOH1180 |
site_id | AC6 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE MS1 A 1002 |
Chain | Residue |
A | GLN450 |
A | ARG452 |
A | ILE453 |
A | ALA541 |
A | PHE542 |
A | PHE545 |
A | ASP547 |
A | SER566 |
A | ALA567 |
A | ARG589 |
A | PHE591 |
A | HOH1021 |
A | HOH1034 |
A | HOH1042 |
A | HOH1065 |
A | HOH1130 |
A | HOH1144 |
A | HOH1145 |
A | HOH1168 |
A | HOH1203 |
B | ARG208 |
B | TYR209 |
B | ILE239 |
B | LYS267 |
B | MET313 |
B | PHE316 |
B | GLY317 |
B | ASP340 |
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:0000250|UniProtKB:P31939 |
Chain | Residue | Details |
A | LYS138 | |
B | LYS138 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor; for AICAR formyltransferase activity => ECO:0000250|UniProtKB:P31939 |
Chain | Residue | Details |
A | HIS268 | |
B | HIS268 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000305|PubMed:11323713, ECO:0000305|PubMed:12501179, ECO:0007744|PDB:1G8M, ECO:0007744|PDB:1M9N |
Chain | Residue | Details |
A | SER13 | |
A | SER35 | |
A | ARG65 | |
A | ASP126 | |
B | SER13 | |
B | SER35 | |
B | ARG65 | |
B | ASP126 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:12501179, ECO:0007744|PDB:1M9N |
Chain | Residue | Details |
A | CYS102 | |
B | CYS102 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | BINDING: in other chain => ECO:0000269|PubMed:12501179, ECO:0007744|PDB:1M9N |
Chain | Residue | Details |
A | ARG208 | |
A | HIS268 | |
A | GLY317 | |
A | ASP340 | |
B | ARG208 | |
B | HIS268 | |
B | GLY317 | |
B | ASP340 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P31939 |
Chain | Residue | Details |
A | ASN432 | |
A | ARG452 | |
B | ASN432 | |
B | ARG452 |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305|PubMed:12974624, ECO:0007744|PDB:1OZ0 |
Chain | Residue | Details |
A | ILE453 | |
A | ASP547 | |
A | SER566 | |
B | ILE453 | |
B | ASP547 | |
B | SER566 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12501179, ECO:0007744|PDB:1M9N |
Chain | Residue | Details |
A | PHE542 | |
A | ARG589 | |
B | PHE542 | |
B | ARG589 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P31939 |
Chain | Residue | Details |
A | LYS267 | |
B | LYS267 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P31939 |
Chain | Residue | Details |
A | LYS200 | |
B | LYS200 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1p4r |
Chain | Residue | Details |
A | HIS593 | |
A | ASN432 | |
A | HIS268 | |
A | LYS267 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1p4r |
Chain | Residue | Details |
B | HIS593 | |
B | ASN432 | |
B | HIS268 | |
B | LYS267 |