6YSP
Arabidopsis aspartate transcarbamoylase complex with PALA and carbamoyl phosphate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004070 | molecular_function | aspartate carbamoyltransferase activity |
A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0016597 | molecular_function | amino acid binding |
A | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
B | 0004070 | molecular_function | aspartate carbamoyltransferase activity |
B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0016597 | molecular_function | amino acid binding |
B | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
C | 0004070 | molecular_function | aspartate carbamoyltransferase activity |
C | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
C | 0006520 | biological_process | amino acid metabolic process |
C | 0016597 | molecular_function | amino acid binding |
C | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue CP A 401 |
Chain | Residue |
A | SER134 |
A | HOH644 |
C | SER163 |
C | HOH510 |
A | THR135 |
A | ARG136 |
A | THR137 |
A | ARG187 |
A | HIS215 |
A | GLN218 |
A | PRO349 |
A | LEU350 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 402 |
Chain | Residue |
A | ARG310 |
A | GLN312 |
A | ARG313 |
A | HOH512 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue GOL A 403 |
Chain | Residue |
A | ILE111 |
A | GLU112 |
A | SER114 |
A | SER116 |
A | GLN117 |
A | SER118 |
A | ARG147 |
A | HOH505 |
C | GLY123 |
site_id | AC4 |
Number of Residues | 12 |
Details | binding site for residue CP B 401 |
Chain | Residue |
A | SER163 |
A | LYS166 |
B | SER134 |
B | THR135 |
B | ARG136 |
B | THR137 |
B | ARG187 |
B | HIS215 |
B | GLN218 |
B | PRO349 |
B | LEU350 |
B | GOL404 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue SO4 B 402 |
Chain | Residue |
B | ARG248 |
B | THR249 |
B | GLN312 |
B | ARG315 |
B | GOL404 |
B | HOH603 |
B | HOH632 |
B | HOH670 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue GOL B 403 |
Chain | Residue |
B | ARG95 |
B | SER99 |
B | GLN227 |
B | LYS232 |
B | LEU233 |
B | ASP234 |
B | HOH507 |
site_id | AC7 |
Number of Residues | 11 |
Details | binding site for residue GOL B 404 |
Chain | Residue |
A | LYS166 |
A | HOH622 |
A | HOH685 |
B | HIS215 |
B | LEU350 |
B | PRO351 |
B | CP401 |
B | SO4402 |
B | HOH511 |
B | HOH528 |
B | HOH603 |
site_id | AC8 |
Number of Residues | 8 |
Details | binding site for residue GOL B 405 |
Chain | Residue |
A | GLY123 |
B | ILE111 |
B | SER114 |
B | SER116 |
B | GLN117 |
B | SER118 |
B | ARG147 |
B | HOH675 |
site_id | AC9 |
Number of Residues | 17 |
Details | binding site for residue PAL C 401 |
Chain | Residue |
B | SER163 |
B | LYS166 |
C | SER134 |
C | THR135 |
C | ARG136 |
C | THR137 |
C | ARG187 |
C | HIS215 |
C | GLN218 |
C | ARG248 |
C | THR249 |
C | ARG310 |
C | GLN312 |
C | LEU350 |
C | PRO351 |
C | HOH586 |
C | HOH587 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue GOL C 402 |
Chain | Residue |
B | GLY123 |
B | LYS342 |
C | ILE111 |
C | SER114 |
C | SER116 |
C | GLN117 |
C | SER118 |
C | ARG147 |
C | HOH522 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue GOL C 403 |
Chain | Residue |
C | ILE331 |
C | HOH504 |
C | HOH566 |
C | HOH634 |
C | LYS329 |
C | PHE330 |
Functional Information from PROSITE/UniProt
site_id | PS00097 |
Number of Residues | 8 |
Details | CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FyEpSTRT |
Chain | Residue | Details |
A | PHE130-THR137 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000269|PubMed:33574254 |
Chain | Residue | Details |
A | ARG136 | |
B | HIS215 | |
B | ARG248 | |
B | ARG310 | |
C | ARG136 | |
C | THR137 | |
C | ARG187 | |
C | HIS215 | |
C | ARG248 | |
C | ARG310 | |
A | THR137 | |
A | ARG187 | |
A | HIS215 | |
A | ARG248 | |
A | ARG310 | |
B | ARG136 | |
B | THR137 | |
B | ARG187 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P0A786 |
Chain | Residue | Details |
A | LYS166 | |
C | GLN218 | |
C | LEU350 | |
C | PRO351 | |
A | GLN218 | |
A | LEU350 | |
A | PRO351 | |
B | LYS166 | |
B | GLN218 | |
B | LEU350 | |
B | PRO351 | |
C | LYS166 |