3R7D
Crystal Structure of Unliganded Aspartate Transcarbamoylase from Bacillus subtilis
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 | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0016597 | molecular_function | amino acid binding |
A | 0016740 | molecular_function | transferase activity |
A | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
A | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
B | 0004070 | molecular_function | aspartate carbamoyltransferase activity |
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 | 0016597 | molecular_function | amino acid binding |
B | 0016740 | molecular_function | transferase activity |
B | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
B | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
C | 0004070 | molecular_function | aspartate carbamoyltransferase activity |
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 | 0016597 | molecular_function | amino acid binding |
C | 0016740 | molecular_function | transferase activity |
C | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
C | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PO4 A 305 |
Chain | Residue |
A | ASN67 |
B | ASN67 |
B | HOH313 |
C | ASN67 |
A | HOH319 |
A | HOH323 |
A | HOH328 |
A | HOH334 |
A | HOH367 |
A | HOH385 |
A | HOH388 |
A | HOH411 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 306 |
Chain | Residue |
A | SER11 |
A | THR12 |
A | ARG171 |
A | HOH312 |
A | HOH343 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 A 307 |
Chain | Residue |
A | THR73 |
A | SER74 |
A | LYS77 |
C | SER47 |
C | THR48 |
C | ARG49 |
C | PRO251 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B 305 |
Chain | Residue |
B | SER11 |
B | THR12 |
B | ARG171 |
B | HOH372 |
B | HOH484 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 C 305 |
Chain | Residue |
C | LYS272 |
C | LYS275 |
C | HOH357 |
C | HOH381 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 C 306 |
Chain | Residue |
C | SER11 |
C | THR12 |
C | ARG171 |
C | HOH359 |
C | HOH573 |
Functional Information from PROSITE/UniProt
site_id | PS00097 |
Number of Residues | 8 |
Details | CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEpSTRT |
Chain | Residue | Details |
A | PHE43-THR50 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 30 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00001 |
Chain | Residue | Details |
A | ARG49 | |
A | PRO251 | |
B | ARG49 | |
B | THR50 | |
B | LYS77 | |
B | ARG99 | |
B | HIS127 | |
B | GLN130 | |
B | ARG160 | |
B | ARG211 | |
B | ALA250 | |
A | THR50 | |
B | PRO251 | |
C | ARG49 | |
C | THR50 | |
C | LYS77 | |
C | ARG99 | |
C | HIS127 | |
C | GLN130 | |
C | ARG160 | |
C | ARG211 | |
C | ALA250 | |
A | LYS77 | |
C | PRO251 | |
A | ARG99 | |
A | HIS127 | |
A | GLN130 | |
A | ARG160 | |
A | ARG211 | |
A | ALA250 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:17218307 |
Chain | Residue | Details |
A | SER303 | |
B | SER303 | |
C | SER303 |