1DUV
CRYSTAL STRUCTURE OF E. COLI ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH NDELTA-L-ORNITHINE-DIAMINOPHOSPHINYL-N-SULPHONIC ACID (PSORN)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| G | 0004585 | molecular_function | ornithine carbamoyltransferase activity |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0006520 | biological_process | amino acid metabolic process |
| G | 0006526 | biological_process | arginine biosynthetic process |
| G | 0006591 | biological_process | ornithine metabolic process |
| G | 0016597 | molecular_function | amino acid binding |
| G | 0016740 | molecular_function | transferase activity |
| G | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| G | 0019240 | biological_process | citrulline biosynthetic process |
| G | 0042450 | biological_process | arginine biosynthetic process via ornithine |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0004585 | molecular_function | ornithine carbamoyltransferase activity |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0006520 | biological_process | amino acid metabolic process |
| H | 0006526 | biological_process | arginine biosynthetic process |
| H | 0006591 | biological_process | ornithine metabolic process |
| H | 0016597 | molecular_function | amino acid binding |
| H | 0016740 | molecular_function | transferase activity |
| H | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| H | 0019240 | biological_process | citrulline biosynthetic process |
| H | 0042450 | biological_process | arginine biosynthetic process via ornithine |
| H | 0046872 | molecular_function | metal ion binding |
| I | 0004585 | molecular_function | ornithine carbamoyltransferase activity |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0006520 | biological_process | amino acid metabolic process |
| I | 0006526 | biological_process | arginine biosynthetic process |
| I | 0006591 | biological_process | ornithine metabolic process |
| I | 0016597 | molecular_function | amino acid binding |
| I | 0016740 | molecular_function | transferase activity |
| I | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| I | 0019240 | biological_process | citrulline biosynthetic process |
| I | 0042450 | biological_process | arginine biosynthetic process via ornithine |
| I | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PSQ G 401 |
| Chain | Residue |
| G | SER55 |
| G | ASN167 |
| G | ASP231 |
| G | SER235 |
| G | MET236 |
| G | CYS273 |
| G | LEU274 |
| G | ARG319 |
| G | HOH606 |
| I | GLN82 |
| I | HOH598 |
| G | THR56 |
| G | ARG57 |
| G | THR58 |
| G | ARG106 |
| G | LEU128 |
| G | HIS133 |
| G | GLN136 |
| G | ASN166 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PSQ H 402 |
| Chain | Residue |
| G | GLN82 |
| H | SER55 |
| H | THR56 |
| H | ARG57 |
| H | THR58 |
| H | ARG106 |
| H | HIS133 |
| H | GLN136 |
| H | ASN166 |
| H | ASN167 |
| H | ASP231 |
| H | SER235 |
| H | MET236 |
| H | CYS273 |
| H | LEU274 |
| H | ARG319 |
| H | HOH602 |
| H | HOH611 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PSQ I 403 |
| Chain | Residue |
| H | GLN82 |
| I | SER55 |
| I | THR56 |
| I | ARG57 |
| I | THR58 |
| I | ARG106 |
| I | HIS133 |
| I | GLN136 |
| I | ASN166 |
| I | ASN167 |
| I | ASP231 |
| I | SER235 |
| I | MET236 |
| I | CYS273 |
| I | LEU274 |
| I | ARG319 |
| I | HOH604 |
| I | HOH773 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD G 404 |
| Chain | Residue |
| G | LEU25 |
| G | ALA329 |
| G | LYS333 |
| G | HOH538 |
| G | HOH1149 |
| H | LYS151 |
Functional Information from PROSITE/UniProt
| site_id | PS00097 |
| Number of Residues | 8 |
| Details | CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FeKdSTRT |
| Chain | Residue | Details |
| G | PHE51-THR58 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 21 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10747936, ECO:0000269|PubMed:9275160, ECO:0007744|PDB:1DUV, ECO:0007744|PDB:2OTC |
| Chain | Residue | Details |
| G | THR56 | |
| H | GLY107 | |
| H | PRO134 | |
| H | MET168 | |
| H | VAL232 | |
| H | MET236 | |
| I | THR56 | |
| I | ILE83 | |
| I | GLY107 | |
| I | PRO134 | |
| I | MET168 | |
| G | ILE83 | |
| I | VAL232 | |
| I | MET236 | |
| G | GLY107 | |
| G | PRO134 | |
| G | MET168 | |
| G | VAL232 | |
| G | MET236 | |
| H | THR56 | |
| H | ILE83 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:2405164 |
| Chain | Residue | Details |
| G | LEU274 | |
| H | LEU274 | |
| I | LEU274 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10747936, ECO:0007744|PDB:1DUV |
| Chain | Residue | Details |
| G | MET320 | |
| H | MET320 | |
| I | MET320 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1akm |
| Chain | Residue | Details |
| G | GLN136 | |
| G | CYS273 | |
| G | ASP231 | |
| G | ARG106 | |
| G | HIS133 | |
| G | ARG319 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1akm |
| Chain | Residue | Details |
| H | GLN136 | |
| H | CYS273 | |
| H | ASP231 | |
| H | ARG106 | |
| H | HIS133 | |
| H | ARG319 |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1akm |
| Chain | Residue | Details |
| I | GLN136 | |
| I | CYS273 | |
| I | ASP231 | |
| I | ARG106 | |
| I | HIS133 | |
| I | ARG319 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1akm |
| Chain | Residue | Details |
| G | THR58 | |
| G | ARG106 | |
| G | HIS133 | |
| G | ARG57 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1akm |
| Chain | Residue | Details |
| H | THR58 | |
| H | ARG106 | |
| H | HIS133 | |
| H | ARG57 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1akm |
| Chain | Residue | Details |
| I | THR58 | |
| I | ARG106 | |
| I | HIS133 | |
| I | ARG57 |
