5VGM
Crystal structure of dihydroorotase pyrC from Vibrio cholerae in complex with zinc at 1.95 A resolution.
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 | 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue ZN A 401 |
Chain | Residue |
A | KCX98 |
A | HIS135 |
A | HIS173 |
A | ZN402 |
A | HOH536 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue ZN A 402 |
Chain | Residue |
A | ZN401 |
A | HOH536 |
A | HIS13 |
A | HIS15 |
A | KCX98 |
A | ASP246 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue ACT A 403 |
Chain | Residue |
A | ARG17 |
A | ASP18 |
A | THR42 |
A | VAL43 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ACT A 404 |
Chain | Residue |
A | ARG203 |
A | ARG223 |
B | ARG203 |
B | ARG223 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue ACT A 405 |
Chain | Residue |
A | ARG303 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue ZN B 401 |
Chain | Residue |
B | KCX98 |
B | HIS135 |
B | HIS173 |
B | ZN402 |
B | HOH556 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue ZN B 402 |
Chain | Residue |
B | HIS13 |
B | HIS15 |
B | KCX98 |
B | ASP246 |
B | ZN401 |
B | HOH556 |
site_id | AC8 |
Number of Residues | 1 |
Details | binding site for residue ACT B 403 |
Chain | Residue |
B | HOH508 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue CL B 404 |
Chain | Residue |
B | GLY282 |
B | LYS283 |
B | LEU284 |
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 |
Chain | Residue | Details |
A | ASP246 | |
B | ASP246 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00219 |
Chain | Residue | Details |
A | HIS13 | |
B | HIS13 | |
B | HIS15 | |
B | ASN41 | |
B | HIS135 | |
B | HIS173 | |
B | LEU218 | |
B | ASP246 | |
B | HIS250 | |
B | ALA262 | |
A | HIS15 | |
A | ASN41 | |
A | HIS135 | |
A | HIS173 | |
A | LEU218 | |
A | ASP246 | |
A | HIS250 | |
A | ALA262 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: via carbamate group => ECO:0000255|HAMAP-Rule:MF_00219 |
Chain | Residue | Details |
A | KCX98 | |
B | KCX98 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_00219 |
Chain | Residue | Details |
A | KCX98 | |
B | KCX98 |