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 | 0008152 | biological_process | metabolic 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 | 0008152 | biological_process | metabolic 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 | ARG65 | |
| A | ASP126 | |
| B | SER13 | |
| B | SER35 | |
| B | ARG65 | |
| B | ASP126 | |
| A | SER13 | |
| A | SER35 |
| 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 |
| B | ARG208 | |
| B | HIS268 | |
| B | GLY317 | |
| B | ASP340 | |
| A | ARG208 | |
| A | HIS268 | |
| A | GLY317 | |
| A | ASP340 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P31939 |
| Chain | Residue | Details |
| B | ASN432 | |
| B | ARG452 | |
| A | ASN432 | |
| A | ARG452 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:12974624, ECO:0007744|PDB:1OZ0 |
| Chain | Residue | Details |
| B | ASP547 | |
| B | SER566 | |
| A | ILE453 | |
| A | ASP547 | |
| A | SER566 | |
| B | ILE453 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12501179, ECO:0007744|PDB:1M9N |
| Chain | Residue | Details |
| B | PHE542 | |
| B | ARG589 | |
| A | PHE542 | |
| A | 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 |
