1XGE
Dihydroorotase from Escherichia coli: Loop Movement and Cooperativity between subunits
Functional 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 | 0042803 | molecular_function | protein homodimerization activity |
| 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 | 0042803 | molecular_function | protein homodimerization activity |
| B | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| B | 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 400 |
| Chain | Residue |
| A | KCX102 |
| A | HIS139 |
| A | HIS177 |
| A | ZN401 |
| A | DOR1410 |
| A | HOH1780 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | ASP250 |
| A | ZN400 |
| A | HOH1780 |
| A | HIS16 |
| A | HIS18 |
| A | KCX102 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 400 |
| Chain | Residue |
| B | KCX102 |
| B | HIS139 |
| B | HIS177 |
| B | NCD2410 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 401 |
| Chain | Residue |
| B | HIS16 |
| B | HIS18 |
| B | KCX102 |
| B | ASP250 |
| B | NCD2410 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE DOR A 1410 |
| Chain | Residue |
| A | HIS18 |
| A | ARG20 |
| A | ASN44 |
| A | HIS139 |
| A | CYS221 |
| A | LEU222 |
| A | HIS254 |
| A | ALA266 |
| A | GLY267 |
| A | ZN400 |
| A | HOH1421 |
| A | HOH1699 |
| A | HOH1780 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NCD B 2410 |
| Chain | Residue |
| B | HIS16 |
| B | HIS18 |
| B | ARG20 |
| B | ASN44 |
| B | KCX102 |
| B | THR109 |
| B | THR110 |
| B | HIS139 |
| B | HIS177 |
| B | CYS221 |
| B | LEU222 |
| B | ASP250 |
| B | ALA252 |
| B | HIS254 |
| B | ALA266 |
| B | GLY267 |
| B | ZN400 |
| B | ZN401 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000305|PubMed:15610022 |
| Chain | Residue | Details |
| A | SER251 | |
| B | SER251 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15826651, ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE |
| Chain | Residue | Details |
| A | LEU17 | |
| B | SER251 | |
| A | LEU19 | |
| A | GLY140 | |
| A | ILE178 | |
| A | SER251 | |
| B | LEU17 | |
| B | LEU19 | |
| B | GLY140 | |
| B | ILE178 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000305|PubMed:11401542, ECO:0000305|PubMed:15826651, ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE |
| Chain | Residue | Details |
| A | LEU45 | |
| A | PRO223 | |
| A | ALA255 | |
| A | GLY267 | |
| B | LEU45 | |
| B | PRO223 | |
| B | ALA255 | |
| B | GLY267 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: via carbamate group => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15826651, ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE |
| Chain | Residue | Details |
| A | LEU103 | |
| B | LEU103 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15826651, ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE |
| Chain | Residue | Details |
| A | LEU103 | |
| B | LEU103 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j79 |
| Chain | Residue | Details |
| A | ASP250 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j79 |
| Chain | Residue | Details |
| B | ASP250 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 630 |
| Chain | Residue | Details |
| A | LEU17 | metal ligand |
| A | LEU19 | metal ligand |
| A | LEU103 | metal ligand |
| A | GLY140 | metal ligand |
| A | ILE178 | metal ligand |
| A | SER251 | metal ligand, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 630 |
| Chain | Residue | Details |
| B | LEU17 | metal ligand |
| B | LEU19 | metal ligand |
| B | LEU103 | metal ligand |
| B | GLY140 | metal ligand |
| B | ILE178 | metal ligand |
| B | SER251 | metal ligand, proton acceptor, proton donor |
