2OGJ
Crystal structure of a dihydroorotase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
A | 0019213 | molecular_function | deacetylase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
B | 0019213 | molecular_function | deacetylase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
C | 0019213 | molecular_function | deacetylase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
D | 0019213 | molecular_function | deacetylase activity |
D | 0046872 | molecular_function | metal ion binding |
E | 0016787 | molecular_function | hydrolase activity |
E | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
E | 0019213 | molecular_function | deacetylase activity |
E | 0046872 | molecular_function | metal ion binding |
F | 0016787 | molecular_function | hydrolase activity |
F | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
F | 0019213 | molecular_function | deacetylase activity |
F | 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 418 |
Chain | Residue |
A | HIS77 |
A | HIS79 |
A | KCX175 |
A | ASP291 |
A | ZN419 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 419 |
Chain | Residue |
A | HOH421 |
A | KCX175 |
A | HIS208 |
A | HIS231 |
A | ZN418 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 500 |
Chain | Residue |
B | HIS77 |
B | HIS79 |
B | KCX175 |
B | ASP291 |
B | ZN501 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 501 |
Chain | Residue |
B | KCX175 |
B | HIS208 |
B | HIS231 |
B | ZN500 |
B | HOH503 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN C 600 |
Chain | Residue |
C | HIS77 |
C | HIS79 |
C | KCX175 |
C | ASP291 |
C | ZN601 |
C | IMD3744 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 601 |
Chain | Residue |
C | KCX175 |
C | HIS208 |
C | HIS231 |
C | ZN600 |
C | IMD3744 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN D 700 |
Chain | Residue |
D | HIS77 |
D | HIS79 |
D | KCX175 |
D | ASP291 |
D | ZN701 |
D | IMD3745 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 701 |
Chain | Residue |
D | KCX175 |
D | HIS208 |
D | HIS231 |
D | ZN700 |
D | IMD3745 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN E 800 |
Chain | Residue |
E | HIS77 |
E | HIS79 |
E | KCX175 |
E | ASP291 |
E | ZN801 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN E 801 |
Chain | Residue |
E | KCX175 |
E | HIS208 |
E | HIS231 |
E | ZN800 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN F 900 |
Chain | Residue |
F | HIS77 |
F | HIS79 |
F | KCX175 |
F | ASP291 |
F | ZN901 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN F 901 |
Chain | Residue |
F | KCX175 |
F | HIS208 |
F | HIS231 |
F | ZN900 |
F | HOH903 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE IMD C 3744 |
Chain | Residue |
C | ASN144 |
C | KCX175 |
C | ARG177 |
C | HIS208 |
C | ZN600 |
C | ZN601 |
C | HOH3749 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE IMD D 3745 |
Chain | Residue |
D | ASN144 |
D | ARG177 |
D | ZN700 |
D | ZN701 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 30 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"23214420","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"23214420","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"23214420","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |