1K1D
Crystal structure of D-hydantoinase
Functional Information from GO Data
| Chain | GOid | namespace | contents | 
| A | 0005737 | cellular_component | cytoplasm | 
| A | 0005829 | cellular_component | cytosol | 
| A | 0016787 | molecular_function | hydrolase activity | 
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | 
| A | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides | 
| A | 0046872 | molecular_function | metal ion binding | 
| B | 0005737 | cellular_component | cytoplasm | 
| B | 0005829 | cellular_component | cytosol | 
| B | 0016787 | molecular_function | hydrolase activity | 
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | 
| B | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides | 
| B | 0046872 | molecular_function | metal ion binding | 
| C | 0005737 | cellular_component | cytoplasm | 
| C | 0005829 | cellular_component | cytosol | 
| C | 0016787 | molecular_function | hydrolase activity | 
| C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | 
| C | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides | 
| C | 0046872 | molecular_function | metal ion binding | 
| D | 0005737 | cellular_component | cytoplasm | 
| D | 0005829 | cellular_component | cytosol | 
| D | 0016787 | molecular_function | hydrolase activity | 
| D | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | 
| D | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides | 
| D | 0046872 | molecular_function | metal ion binding | 
| E | 0005737 | cellular_component | cytoplasm | 
| E | 0005829 | cellular_component | cytosol | 
| E | 0016787 | molecular_function | hydrolase activity | 
| E | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | 
| E | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides | 
| E | 0046872 | molecular_function | metal ion binding | 
| F | 0005737 | cellular_component | cytoplasm | 
| F | 0005829 | cellular_component | cytosol | 
| F | 0016787 | molecular_function | hydrolase activity | 
| F | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | 
| F | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides | 
| F | 0046872 | molecular_function | metal ion binding | 
| G | 0005737 | cellular_component | cytoplasm | 
| G | 0005829 | cellular_component | cytosol | 
| G | 0016787 | molecular_function | hydrolase activity | 
| G | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | 
| G | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides | 
| G | 0046872 | molecular_function | metal ion binding | 
| H | 0005737 | cellular_component | cytoplasm | 
| H | 0005829 | cellular_component | cytosol | 
| H | 0016787 | molecular_function | hydrolase activity | 
| H | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | 
| H | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides | 
| H | 0046872 | molecular_function | metal ion binding | 
Functional Information from PDB Data
| site_id | AC1 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE ZN A 501 | 
| Chain | Residue | 
| A | KCX150 | 
| A | HIS183 | 
| A | HIS239 | 
| A | ZN502 | 
| site_id | AC2 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE ZN A 502 | 
| Chain | Residue | 
| A | HIS58 | 
| A | HIS60 | 
| A | KCX150 | 
| A | ASP315 | 
| A | ZN501 | 
| site_id | AC3 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE ZN B 501 | 
| Chain | Residue | 
| B | KCX150 | 
| B | HIS183 | 
| B | HIS239 | 
| B | ZN502 | 
| site_id | AC4 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE ZN B 502 | 
| Chain | Residue | 
| B | HIS58 | 
| B | HIS60 | 
| B | KCX150 | 
| B | ASP315 | 
| B | ZN501 | 
| site_id | AC5 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE ZN C 501 | 
| Chain | Residue | 
| C | KCX150 | 
| C | HIS183 | 
| C | HIS239 | 
| C | ZN502 | 
| site_id | AC6 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE ZN C 502 | 
| Chain | Residue | 
| C | HIS58 | 
| C | HIS60 | 
| C | KCX150 | 
| C | ASP315 | 
| C | ZN501 | 
| site_id | AC7 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE ZN D 501 | 
| Chain | Residue | 
| D | KCX150 | 
| D | HIS183 | 
| D | HIS239 | 
| D | ZN502 | 
| site_id | AC8 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE ZN D 502 | 
| Chain | Residue | 
| D | HIS58 | 
| D | HIS60 | 
| D | KCX150 | 
| D | ASP315 | 
| D | ZN501 | 
| site_id | AC9 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE ZN E 501 | 
| Chain | Residue | 
| E | KCX150 | 
| E | HIS183 | 
| E | HIS239 | 
| E | ZN502 | 
| site_id | BC1 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE ZN E 502 | 
| Chain | Residue | 
| E | HIS58 | 
| E | HIS60 | 
| E | KCX150 | 
| E | ASP315 | 
| E | ZN501 | 
| site_id | BC2 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE ZN F 501 | 
| Chain | Residue | 
| F | KCX150 | 
| F | HIS183 | 
| F | HIS239 | 
| F | ZN502 | 
| site_id | BC3 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE ZN F 502 | 
| Chain | Residue | 
| F | HIS58 | 
| F | HIS60 | 
| F | KCX150 | 
| F | ASP315 | 
| F | ZN501 | 
| site_id | BC4 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE ZN G 501 | 
| Chain | Residue | 
| G | KCX150 | 
| G | HIS183 | 
| G | HIS239 | 
| G | ZN502 | 
| site_id | BC5 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE ZN G 502 | 
| Chain | Residue | 
| G | HIS58 | 
| G | HIS60 | 
| G | KCX150 | 
| G | ASP315 | 
| G | ZN501 | 
| site_id | BC6 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE ZN H 501 | 
| Chain | Residue | 
| H | KCX150 | 
| H | HIS183 | 
| H | HIS239 | 
| H | ZN502 | 
| site_id | BC7 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE ZN H 502 | 
| Chain | Residue | 
| H | HIS58 | 
| H | HIS60 | 
| H | KCX150 | 
| H | ASP315 | 
| H | ZN501 | 
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 | 
| Number of Residues | 40 | 
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12135362","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K1D","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 8 | 
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"12135362","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K1D","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI3 | 
| Number of Residues | 24 | 
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9P903","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI4 | 
| Number of Residues | 8 | 
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"12135362","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
Catalytic Information from CSA
| site_id | CSA1 | 
| Number of Residues | 1 | 
| Details | Annotated By Reference To The Literature 1j79 | 
| Chain | Residue | Details | 
| A | ASP315 | 
| site_id | CSA2 | 
| Number of Residues | 1 | 
| Details | Annotated By Reference To The Literature 1j79 | 
| Chain | Residue | Details | 
| B | ASP315 | 
| site_id | CSA3 | 
| Number of Residues | 1 | 
| Details | Annotated By Reference To The Literature 1j79 | 
| Chain | Residue | Details | 
| C | ASP315 | 
| site_id | CSA4 | 
| Number of Residues | 1 | 
| Details | Annotated By Reference To The Literature 1j79 | 
| Chain | Residue | Details | 
| D | ASP315 | 
| site_id | CSA5 | 
| Number of Residues | 1 | 
| Details | Annotated By Reference To The Literature 1j79 | 
| Chain | Residue | Details | 
| E | ASP315 | 
| site_id | CSA6 | 
| Number of Residues | 1 | 
| Details | Annotated By Reference To The Literature 1j79 | 
| Chain | Residue | Details | 
| F | ASP315 | 
| site_id | CSA7 | 
| Number of Residues | 1 | 
| Details | Annotated By Reference To The Literature 1j79 | 
| Chain | Residue | Details | 
| G | ASP315 | 
| site_id | CSA8 | 
| Number of Residues | 1 | 
| Details | Annotated By Reference To The Literature 1j79 | 
| Chain | Residue | Details | 
| H | ASP315 | 






