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 |
