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6SXU

GH51 a-l-arabinofuranosidase soaked with cyclic sulfate inhibitor

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0000272biological_processpolysaccharide catabolic process
AAA0005737cellular_componentcytoplasm
AAA0016798molecular_functionhydrolase activity, acting on glycosyl bonds
AAA0031222biological_processarabinan catabolic process
AAA0046373biological_processL-arabinose metabolic process
AAA0046556molecular_functionalpha-L-arabinofuranosidase activity
BBB0000272biological_processpolysaccharide catabolic process
BBB0005737cellular_componentcytoplasm
BBB0016798molecular_functionhydrolase activity, acting on glycosyl bonds
BBB0031222biological_processarabinan catabolic process
BBB0046373biological_processL-arabinose metabolic process
BBB0046556molecular_functionalpha-L-arabinofuranosidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor
ChainResidueDetails
AAAGLU175
BBBGLU175

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AAAGLU294
BBBGLU294

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AAAGLU29
AAAASN74
AAATYR246
AAAGLU294
BBBGLU29
BBBASN74
BBBTYR246
BBBGLU294

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AAAASN174
AAAGLN351
BBBASN174
BBBGLN351

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Important for substrate recognition => ECO:0000305
ChainResidueDetails
AAATRP298
AAAGLN351
BBBTRP298
BBBGLN351

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 667
ChainResidueDetails
AAAGLU175activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
AAAGLU294covalently attached, nucleofuge, nucleophile

site_idMCSA2
Number of Residues2
DetailsM-CSA 667
ChainResidueDetails
BBBGLU175activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
BBBGLU294covalently attached, nucleofuge, nucleophile

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PDB entries from 2024-07-17

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