2EG7
The crystal structure of E. coli dihydroorotase complexed with HDDP
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 | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 400 |
Chain | Residue |
A | KCX102 |
A | HIS139 |
A | HIS177 |
A | ZN401 |
A | OTD410 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 401 |
Chain | Residue |
A | ZN400 |
A | OTD410 |
A | HIS16 |
A | HIS18 |
A | KCX102 |
A | ASP250 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 400 |
Chain | Residue |
B | HIS16 |
B | HIS18 |
B | KCX102 |
B | ASP250 |
B | ZN401 |
B | OTD410 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 401 |
Chain | Residue |
B | KCX102 |
B | HIS139 |
B | HIS177 |
B | ZN400 |
B | OTD410 |
site_id | AC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE OTD A 410 |
Chain | Residue |
A | HIS16 |
A | HIS18 |
A | ARG20 |
A | ASN44 |
A | KCX102 |
A | HIS139 |
A | HIS177 |
A | CYS221 |
A | LEU222 |
A | ASP250 |
A | ALA252 |
A | HIS254 |
A | ALA266 |
A | GLY267 |
A | ZN400 |
A | ZN401 |
A | HOH591 |
site_id | AC6 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE OTD B 410 |
Chain | Residue |
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 | ASP250 | |
B | ASP250 |
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 | HIS16 | |
B | ASP250 | |
A | HIS18 | |
A | HIS139 | |
A | HIS177 | |
A | ASP250 | |
B | HIS16 | |
B | HIS18 | |
B | HIS139 | |
B | HIS177 |
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 | ASN44 | |
A | LEU222 | |
A | HIS254 | |
A | ALA266 | |
B | ASN44 | |
B | LEU222 | |
B | HIS254 | |
B | ALA266 |
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 | KCX102 | |
B | KCX102 |
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 | KCX102 | |
B | KCX102 |
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 | HIS16 | metal ligand |
A | HIS18 | metal ligand |
A | KCX102 | metal ligand |
A | HIS139 | metal ligand |
A | HIS177 | metal ligand |
A | ASP250 | metal ligand, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 630 |
Chain | Residue | Details |
B | HIS16 | metal ligand |
B | HIS18 | metal ligand |
B | KCX102 | metal ligand |
B | HIS139 | metal ligand |
B | HIS177 | metal ligand |
B | ASP250 | metal ligand, proton acceptor, proton donor |