3JZE
1.8 Angstrom resolution crystal structure of dihydroorotase (pyrC) from Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Replaces: 3IHNFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004151 | molecular_function | dihydroorotase activity |
| 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 | 0008270 | molecular_function | zinc ion binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
| A | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| A | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004151 | molecular_function | dihydroorotase activity |
| 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 | 0008270 | molecular_function | zinc ion binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
| B | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| B | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004151 | molecular_function | dihydroorotase activity |
| 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 | 0008270 | molecular_function | zinc ion binding |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
| C | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| C | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004151 | molecular_function | dihydroorotase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| 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 | 0016787 | molecular_function | hydrolase activity |
| D | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
| D | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| D | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | HIS17 |
| A | HIS19 |
| A | KCX103 |
| A | ASP251 |
| A | ZN402 |
| A | HOH419 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 402 |
| Chain | Residue |
| A | ZN401 |
| A | HOH419 |
| A | KCX103 |
| A | HIS140 |
| A | HIS178 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME A 411 |
| Chain | Residue |
| A | CYS264 |
| A | GLY265 |
| A | BME415 |
| B | GLY214 |
| B | GLY215 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME A 415 |
| Chain | Residue |
| A | HIS255 |
| A | CYS266 |
| A | BME411 |
| A | HOH570 |
| A | HOH915 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PGE A 420 |
| Chain | Residue |
| A | LYS173 |
| A | ASP193 |
| A | TYR194 |
| A | GLN302 |
| A | PHE303 |
| A | GLY305 |
| A | HOH764 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACY A 423 |
| Chain | Residue |
| A | HIS19 |
| A | ARG21 |
| A | ASN45 |
| A | THR110 |
| A | THR111 |
| A | ALA253 |
| A | HIS255 |
| A | ALA267 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 403 |
| Chain | Residue |
| B | HIS17 |
| B | HIS19 |
| B | KCX103 |
| B | ASP251 |
| B | ZN404 |
| B | HOH1334 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN B 404 |
| Chain | Residue |
| B | KCX103 |
| B | HIS140 |
| B | HIS178 |
| B | ZN403 |
| B | ACY428 |
| B | HOH435 |
| B | HOH1334 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME B 413 |
| Chain | Residue |
| A | GLY214 |
| A | GLY215 |
| B | CYS264 |
| B | GLY265 |
| B | BME417 |
| B | HOH453 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME B 417 |
| Chain | Residue |
| B | HIS255 |
| B | CYS266 |
| B | BME413 |
| B | HOH444 |
| B | HOH1152 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PG4 B 419 |
| Chain | Residue |
| B | LYS173 |
| B | ASP193 |
| B | TYR194 |
| B | GLN302 |
| B | PHE303 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACY B 425 |
| Chain | Residue |
| B | HIS19 |
| B | ARG21 |
| B | ASN45 |
| B | HIS255 |
| B | ALA267 |
| B | HOH371 |
| B | ACY428 |
| B | HOH575 |
| B | HOH1023 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACY B 428 |
| Chain | Residue |
| B | KCX103 |
| B | TYR105 |
| B | HIS140 |
| B | HOH371 |
| B | ZN404 |
| B | ACY425 |
| B | HOH435 |
| B | HOH575 |
| B | HOH1334 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN C 405 |
| Chain | Residue |
| C | HIS17 |
| C | HIS19 |
| C | KCX103 |
| C | ASP251 |
| C | ZN406 |
| C | HOH1333 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 406 |
| Chain | Residue |
| C | KCX103 |
| C | HIS140 |
| C | HIS178 |
| C | ZN405 |
| C | HOH1333 |
| site_id | BC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL C 409 |
| Chain | Residue |
| C | ARG228 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME C 412 |
| Chain | Residue |
| C | CYS264 |
| C | BME416 |
| D | GLY214 |
| D | GLY215 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME C 416 |
| Chain | Residue |
| C | CYS266 |
| C | BME412 |
| C | HOH786 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PGE C 421 |
| Chain | Residue |
| C | LYS173 |
| C | ASP193 |
| C | PHE303 |
| C | HOH688 |
| C | HOH744 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACY C 424 |
| Chain | Residue |
| C | HIS19 |
| C | ARG21 |
| C | ASN45 |
| C | THR111 |
| C | ALA253 |
| C | HIS255 |
| C | ALA267 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN D 407 |
| Chain | Residue |
| D | HIS17 |
| D | HIS19 |
| D | KCX103 |
| D | ASP251 |
| D | ZN408 |
| D | HOH925 |
| site_id | CC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN D 408 |
| Chain | Residue |
| D | KCX103 |
| D | HIS140 |
| D | HIS178 |
| D | ZN407 |
| D | ACY427 |
| D | HOH435 |
| D | HOH925 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME D 414 |
| Chain | Residue |
| C | GLY214 |
| C | GLY215 |
| D | CYS264 |
| D | GLY265 |
| D | BME418 |
| D | HOH452 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME D 418 |
| Chain | Residue |
| D | HIS255 |
| D | CYS266 |
| D | BME414 |
| D | ACY426 |
| site_id | CC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PG4 D 422 |
| Chain | Residue |
| D | GLY134 |
| D | LYS173 |
| D | ASP193 |
| D | TYR194 |
| D | GLN302 |
| D | PHE303 |
| D | GLY305 |
| D | HOH887 |
| site_id | CC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACY D 426 |
| Chain | Residue |
| D | HIS19 |
| D | ARG21 |
| D | ASN45 |
| D | HIS255 |
| D | ALA267 |
| D | BME418 |
| D | ACY427 |
| site_id | CC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ACY D 427 |
| Chain | Residue |
| D | ASN45 |
| D | KCX103 |
| D | TYR105 |
| D | HIS140 |
| D | ZN408 |
| D | ACY426 |
| D | HOH435 |
| D | HOH671 |
| D | HOH925 |
| D | HOH1119 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00219 |
| Chain | Residue | Details |
| A | ASP251 | |
| B | ASP251 | |
| C | ASP251 | |
| D | ASP251 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|Ref.3, ECO:0007744|PDB:3JZE |
| Chain | Residue | Details |
| A | HIS17 | |
| B | ASP251 | |
| C | HIS17 | |
| C | HIS19 | |
| C | HIS140 | |
| C | HIS178 | |
| C | ASP251 | |
| D | HIS17 | |
| D | HIS19 | |
| D | HIS140 | |
| D | HIS178 | |
| A | HIS19 | |
| D | ASP251 | |
| A | HIS140 | |
| A | HIS178 | |
| A | ASP251 | |
| B | HIS17 | |
| B | HIS19 | |
| B | HIS140 | |
| B | HIS178 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00219 |
| Chain | Residue | Details |
| A | ASN45 | |
| C | LEU223 | |
| C | HIS255 | |
| C | ALA267 | |
| D | ASN45 | |
| D | LEU223 | |
| D | HIS255 | |
| D | ALA267 | |
| A | LEU223 | |
| A | HIS255 | |
| A | ALA267 | |
| B | ASN45 | |
| B | LEU223 | |
| B | HIS255 | |
| B | ALA267 | |
| C | ASN45 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: via carbamate group => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|Ref.3, ECO:0007744|PDB:3JZE |
| Chain | Residue | Details |
| A | KCX103 | |
| B | KCX103 | |
| C | KCX103 | |
| D | KCX103 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_00219 |
| Chain | Residue | Details |
| A | KCX103 | |
| B | KCX103 | |
| C | KCX103 | |
| D | KCX103 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j79 |
| Chain | Residue | Details |
| A | ASP251 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j79 |
| Chain | Residue | Details |
| B | ASP251 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j79 |
| Chain | Residue | Details |
| C | ASP251 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j79 |
| Chain | Residue | Details |
| D | ASP251 |
