3R7F
Crystal Structure of CP-bound 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 | 11 |
| Details | BINDING SITE FOR RESIDUE CP A 802 |
| Chain | Residue |
| A | SER47 |
| A | HOH511 |
| B | SER74 |
| A | THR48 |
| A | ARG49 |
| A | THR50 |
| A | ARG99 |
| A | HIS127 |
| A | GLN130 |
| A | PRO249 |
| A | ALA250 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 305 |
| Chain | Residue |
| A | ASN67 |
| A | HOH438 |
| A | HOH446 |
| A | HOH447 |
| A | HOH478 |
| A | HOH604 |
| A | HOH606 |
| B | ASN67 |
| C | ASN67 |
| C | HOH340 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 306 |
| Chain | Residue |
| A | LYS59 |
| A | HOH317 |
| A | HOH344 |
| A | HOH478 |
| A | HOH497 |
| A | HOH604 |
| A | HOH606 |
| B | LYS59 |
| C | LYS59 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 307 |
| Chain | Residue |
| A | SER11 |
| A | THR12 |
| A | ARG171 |
| A | HOH418 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 308 |
| Chain | Residue |
| A | GLN23 |
| A | LYS26 |
| A | GLU140 |
| A | LYS272 |
| A | HOH463 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 309 |
| Chain | Residue |
| A | LYS272 |
| A | LYS275 |
| A | HOH406 |
| A | HOH424 |
| A | HOH429 |
| A | HOH468 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 310 |
| Chain | Residue |
| A | LYS241 |
| A | ARG242 |
| A | HIS243 |
| A | HOH379 |
| A | HOH403 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CP B 802 |
| Chain | Residue |
| B | SER47 |
| B | THR48 |
| B | ARG49 |
| B | THR50 |
| B | ARG99 |
| B | HIS127 |
| B | GLN130 |
| B | PRO249 |
| B | ALA250 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 305 |
| Chain | Residue |
| B | GLN23 |
| B | LYS26 |
| B | GLU140 |
| B | LYS272 |
| B | HOH380 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 306 |
| Chain | Residue |
| B | SER11 |
| B | THR12 |
| B | ARG171 |
| B | HOH411 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 307 |
| Chain | Residue |
| B | LYS272 |
| B | LYS275 |
| B | HOH392 |
| B | HOH393 |
| B | HOH414 |
| B | HOH459 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CP B 308 |
| Chain | Residue |
| A | HOH329 |
| B | THR144 |
| B | PHE145 |
| B | LYS146 |
| B | HOH350 |
| B | HOH368 |
| B | HOH501 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CP C 802 |
| Chain | Residue |
| C | SER47 |
| C | THR48 |
| C | ARG49 |
| C | THR50 |
| C | ARG99 |
| C | HIS127 |
| C | GLN130 |
| C | PRO249 |
| C | ALA250 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 C 305 |
| Chain | Residue |
| C | GLN23 |
| C | LYS26 |
| C | GLU140 |
| C | LYS272 |
| C | HOH572 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 C 306 |
| Chain | Residue |
| C | HOH389 |
| C | HOH405 |
| C | LYS272 |
| C | LYS275 |
| C | HOH382 |
| C | HOH383 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 C 307 |
| Chain | Residue |
| C | SER11 |
| C | THR12 |
| C | ARG171 |
| C | HOH363 |
| C | HOH615 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 C 308 |
| Chain | Residue |
| C | LYS16 |
| C | TYR139 |
| C | THR144 |
| C | PHE145 |
| C | LYS146 |
| C | HOH359 |
| C | HOH621 |
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 | PRO251 | |
| B | ARG49 | |
| B | THR50 | |
| B | LYS77 | |
| B | ARG99 | |
| B | HIS127 | |
| B | GLN130 | |
| B | ARG160 | |
| B | ARG211 | |
| B | ALA250 | |
| B | PRO251 | |
| C | ARG49 | |
| C | THR50 | |
| C | LYS77 | |
| C | ARG99 | |
| C | HIS127 | |
| C | GLN130 | |
| C | ARG160 | |
| C | ARG211 | |
| C | ALA250 | |
| C | PRO251 | |
| A | ARG99 | |
| A | HIS127 | |
| A | GLN130 | |
| A | ARG160 | |
| A | ARG211 | |
| A | ALA250 | |
| A | ARG49 | |
| A | THR50 | |
| A | LYS77 |
| 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 |
