1EKX
THE ISOLATED, UNREGULATED CATALYTIC TRIMER OF ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH BISUBSTRATE ANALOG PALA (N-(PHOSPHONACETYL)-L-ASPARTATE)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004070 | molecular_function | aspartate carbamoyltransferase activity |
A | 0004088 | molecular_function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0006541 | biological_process | glutamine metabolic process |
A | 0009347 | cellular_component | aspartate carbamoyltransferase complex |
A | 0016597 | molecular_function | amino acid binding |
A | 0016740 | molecular_function | transferase activity |
A | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
A | 0070207 | biological_process | protein homotrimerization |
B | 0004070 | molecular_function | aspartate carbamoyltransferase activity |
B | 0004088 | molecular_function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0006541 | biological_process | glutamine metabolic process |
B | 0009347 | cellular_component | aspartate carbamoyltransferase complex |
B | 0016597 | molecular_function | amino acid binding |
B | 0016740 | molecular_function | transferase activity |
B | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
B | 0070207 | biological_process | protein homotrimerization |
C | 0004070 | molecular_function | aspartate carbamoyltransferase activity |
C | 0004088 | molecular_function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
C | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
C | 0006520 | biological_process | amino acid metabolic process |
C | 0006541 | biological_process | glutamine metabolic process |
C | 0009347 | cellular_component | aspartate carbamoyltransferase complex |
C | 0016597 | molecular_function | amino acid binding |
C | 0016740 | molecular_function | transferase activity |
C | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
C | 0042802 | molecular_function | identical protein binding |
C | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
C | 0070207 | biological_process | protein homotrimerization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA C 311 |
Chain | Residue |
C | ARG113 |
C | ASN132 |
C | HOH1048 |
C | HOH1154 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 311 |
Chain | Residue |
C | ASP253 |
B | ASP153 |
B | HOH1078 |
B | HOH1173 |
B | HOH1209 |
C | GLU216 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PAL A 1001 |
Chain | Residue |
A | SER52 |
A | THR53 |
A | ARG54 |
A | THR55 |
A | ARG105 |
A | HIS134 |
A | ARG167 |
A | ARG229 |
A | GLN231 |
A | LEU267 |
A | HOH1005 |
A | HOH1007 |
B | SER80 |
B | LYS84 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE PAL B 1002 |
Chain | Residue |
B | SER52 |
B | THR53 |
B | ARG54 |
B | THR55 |
B | ARG105 |
B | HIS134 |
B | GLN137 |
B | ARG167 |
B | ARG229 |
B | GLN231 |
B | LEU267 |
B | HOH1004 |
B | HOH1006 |
C | SER80 |
C | LYS84 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PAL C 1003 |
Chain | Residue |
A | SER80 |
A | LYS84 |
C | SER52 |
C | THR53 |
C | ARG54 |
C | THR55 |
C | ARG105 |
C | HIS134 |
C | ARG167 |
C | ARG229 |
C | GLN231 |
C | LEU267 |
C | HOH1008 |
C | HOH1030 |
Functional Information from PROSITE/UniProt
site_id | PS00097 |
Number of Residues | 8 |
Details | CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEaSTRT |
Chain | Residue | Details |
A | PHE48-THR55 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 21 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000269|PubMed:3380787 |
Chain | Residue | Details |
A | ARG54 | |
B | ARG105 | |
B | HIS134 | |
B | GLN137 | |
B | LEU267 | |
B | PRO268 | |
C | ARG54 | |
C | THR55 | |
C | ARG105 | |
C | HIS134 | |
C | GLN137 | |
A | THR55 | |
C | LEU267 | |
C | PRO268 | |
A | ARG105 | |
A | HIS134 | |
A | GLN137 | |
A | LEU267 | |
A | PRO268 | |
B | ARG54 | |
B | THR55 |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 |
Chain | Residue | Details |
A | LYS84 | |
A | ARG167 | |
A | ARG229 | |
B | LYS84 | |
B | ARG167 | |
B | ARG229 | |
C | LYS84 | |
C | ARG167 | |
C | ARG229 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1at1 |
Chain | Residue | Details |
A | ARG54 | |
A | HIS134 | |
A | ARG105 | |
A | THR55 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1at1 |
Chain | Residue | Details |
B | ARG54 | |
B | HIS134 | |
B | ARG105 | |
B | THR55 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1at1 |
Chain | Residue | Details |
C | ARG54 | |
C | HIS134 | |
C | ARG105 | |
C | THR55 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 405 |
Chain | Residue | Details |
A | ARG54 | electrostatic stabiliser |
A | THR55 | electrostatic stabiliser, increase electrophilicity |
A | LYS84 | proton shuttle (general acid/base) |
A | ARG105 | electrostatic stabiliser, increase electrophilicity |
A | HIS134 | electrostatic stabiliser, increase electrophilicity |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 405 |
Chain | Residue | Details |
B | ARG54 | electrostatic stabiliser |
B | THR55 | electrostatic stabiliser, increase electrophilicity |
B | LYS84 | proton shuttle (general acid/base) |
B | ARG105 | electrostatic stabiliser, increase electrophilicity |
B | HIS134 | electrostatic stabiliser, increase electrophilicity |
site_id | MCSA3 |
Number of Residues | 5 |
Details | M-CSA 405 |
Chain | Residue | Details |
C | ARG54 | electrostatic stabiliser |
C | THR55 | electrostatic stabiliser, increase electrophilicity |
C | LYS84 | proton shuttle (general acid/base) |
C | ARG105 | electrostatic stabiliser, increase electrophilicity |
C | HIS134 | electrostatic stabiliser, increase electrophilicity |