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Search The CSA
PDB ID
UNIPROT ID
EC Number

Catalytic Site Atlas

CSA LITERATURE entry for 1dw9

E.C. namecyanase
SpeciesEscherichia coli (Bacteria)
E.C. Number (IntEnz) 4.2.1.104
CSA Homologues of 1dw91dwk,
CSA Entries With UniProtID P00816
CSA Entries With EC Number 4.2.1.104
PDBe Entry 1dw9
PDBSum Entry 1dw9
MACiE Entry 1dw9

Literature Report

IntroductionCyanate lyase activity is present in some but not all bacteria. The enzyme detoxifies the cyanate ion, which reacts with nucleophilic groups of proteins. The enzyme is a decamer with unusual 5/2 (D2) symmetry, forming a pentamer of dimers. The active site is dyadic and made up of residues from two adjacent dimers. There are 5 active sites per decamer. The protein fold is unique but shows some similarity to DNA binding proteins such as 434 repressor, but the enzyme is not thought to bind DNA in vivo.
MechansimUnknown, but the active site is made up of residues from two adjacent dimers. Conserved residues in the active site are B Arg96, G Arg96, E Ser122, F Ser122, B GLu99, G Glu99 to form a dyadic active site.
Reaction

Catalytic Sites for 1dw9

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluA9999macie:sideChain
ArgF9696macie:sideChain

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluG9999macie:sideChain
ArgB9696macie:sideChain

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ArgG9696macie:sideChain
GluB9999macie:sideChain

Annotated By Reference To The Literature - Site 4 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluC9999macie:sideChain
ArgE9696macie:sideChain

Annotated By Reference To The Literature - Site 5 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ArgD9696macie:sideChain
GluI9999macie:sideChain

Annotated By Reference To The Literature - Site 6 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluD9999macie:sideChain
ArgI9696macie:sideChain

Annotated By Reference To The Literature - Site 7 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluH9999macie:sideChain
ArgJ9696macie:sideChain

Annotated By Reference To The Literature - Site 8 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ArgH9696macie:sideChain
GluJ9999macie:sideChain

Annotated By Reference To The Literature - Site 9 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ArgA9696macie:sideChain
GluF9999macie:sideChain

Literature References

Notes:
Walsh MA
Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site.
Structure 2000 8 505-514
PubMed: 10801492
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