1RAG
CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY
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 | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
B | 0008270 | molecular_function | zinc ion binding |
B | 0009347 | cellular_component | aspartate carbamoyltransferase complex |
B | 0046872 | molecular_function | metal ion binding |
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 |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
D | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
D | 0008270 | molecular_function | zinc ion binding |
D | 0009347 | cellular_component | aspartate carbamoyltransferase complex |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 154 |
Chain | Residue |
B | CYS114 |
B | CYS138 |
B | CYS141 |
B | CYS109 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 154 |
Chain | Residue |
D | CYS109 |
D | CYS114 |
D | CYS138 |
D | CYS141 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE CTP B 999 |
Chain | Residue |
B | VAL9 |
B | ALA11 |
B | ILE12 |
B | VAL17 |
B | HIS20 |
B | LYS60 |
B | ILE86 |
B | TYR89 |
B | VAL91 |
B | LYS94 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CTP D 999 |
Chain | Residue |
D | GLU10 |
D | ALA11 |
D | ILE12 |
D | ASP19 |
D | GLU52 |
D | THR82 |
D | ASN84 |
D | TYR89 |
D | GLU90 |
D | VAL91 |
D | LYS94 |
site_id | ZNB |
Number of Residues | 4 |
Details | ZN BINDING SITE OF CHAIN B |
Chain | Residue |
B | CYS109 |
B | CYS114 |
B | CYS138 |
B | CYS141 |
site_id | ZND |
Number of Residues | 4 |
Details | ZN BINDING SITE OF CHAIN D |
Chain | Residue |
D | CYS109 |
D | CYS114 |
D | CYS138 |
D | CYS141 |
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 | 8 |
Details | BINDING: |
Chain | Residue | Details |
B | CYS109 | |
C | ARG105 | |
C | HIS134 | |
C | GLN137 | |
C | LEU267 | |
C | PRO268 | |
B | CYS114 | |
B | CYS138 | |
B | CYS141 | |
D | CYS109 | |
D | CYS114 | |
D | CYS138 | |
D | CYS141 | |
C | THR55 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 |
Chain | Residue | Details |
A | LYS84 | |
A | ARG167 | |
A | 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 |
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 |
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 |