1M9N
CRYSTAL STRUCTURE OF THE HOMODIMERIC BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME AVIAN ATIC IN COMPLEX WITH AICAR AND XMP AT 1.93 ANGSTROMS.
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 A 594 |
Chain | Residue |
A | VAL426 |
A | THR429 |
A | SER431 |
A | SER433 |
A | ASP540 |
A | LEU590 |
A | HIS592 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE K B 594 |
Chain | Residue |
B | SER431 |
B | SER433 |
B | ASP540 |
B | LEU590 |
B | HIS592 |
B | VAL426 |
B | THR429 |
site_id | AC3 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE AMZ A 1001 |
Chain | Residue |
A | ARG208 |
A | TYR209 |
A | ILE239 |
A | ASN240 |
A | LYS267 |
A | HIS268 |
A | GLY317 |
A | ASP340 |
A | HOH1004 |
A | HOH1005 |
A | HOH1013 |
A | HOH1022 |
A | HOH1054 |
A | HOH1080 |
A | HOH1136 |
A | HOH1145 |
A | HOH1161 |
B | ALA541 |
B | PHE542 |
B | ARG589 |
B | PHE591 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE AMZ B 1002 |
Chain | Residue |
A | PHE542 |
A | ARG589 |
B | ARG208 |
B | TYR209 |
B | ILE239 |
B | ASN240 |
B | LYS267 |
B | HIS268 |
B | GLY317 |
B | ASP340 |
B | HOH1005 |
B | HOH1006 |
B | HOH1008 |
B | HOH1017 |
B | HOH1028 |
B | HOH1042 |
site_id | AC5 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE XMP A 1003 |
Chain | Residue |
A | SER11 |
A | VAL12 |
A | SER13 |
A | LYS15 |
A | SER35 |
A | GLY37 |
A | THR38 |
A | GLY64 |
A | ARG65 |
A | LYS67 |
A | THR68 |
A | LEU69 |
A | CYS102 |
A | ASN103 |
A | LEU104 |
A | TYR105 |
A | ASP126 |
A | ILE127 |
A | GLY128 |
A | GLY129 |
site_id | AC6 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE XMP B 1004 |
Chain | Residue |
B | SER11 |
B | VAL12 |
B | SER13 |
B | LYS15 |
B | SER35 |
B | GLY37 |
B | THR38 |
B | GLY64 |
B | ARG65 |
B | LYS67 |
B | THR68 |
B | CYS102 |
B | ASN103 |
B | LEU104 |
B | TYR105 |
B | ASP126 |
B | ILE127 |
B | GLY128 |
B | GLY129 |
B | HOH1036 |
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 |