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6SXV

GH51 a-l-arabinofuranosidase soaked with aziridine inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0005737cellular_componentcytoplasm
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031222biological_processarabinan catabolic process
A0046373biological_processL-arabinose metabolic process
A0046556molecular_functionalpha-L-arabinofuranosidase activity
B0000272biological_processpolysaccharide catabolic process
B0005737cellular_componentcytoplasm
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031222biological_processarabinan catabolic process
B0046373biological_processL-arabinose metabolic process
B0046556molecular_functionalpha-L-arabinofuranosidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor
ChainResidueDetails
AGLU175
BGLU175

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AGLU294
BGLU294

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AGLU29
AASN74
ATYR246
AGLU294
BGLU29
BASN74
BTYR246
BGLU294

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASN174
AGLN351
BASN174
BGLN351

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Important for substrate recognition => ECO:0000305
ChainResidueDetails
ATRP298
AGLN351
BTRP298
BGLN351

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 667
ChainResidueDetails
AGLU175activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
AGLU294covalently attached, nucleofuge, nucleophile

site_idMCSA2
Number of Residues2
DetailsM-CSA 667
ChainResidueDetails
BGLU175activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
BGLU294covalently attached, nucleofuge, nucleophile

221716

PDB entries from 2024-06-26

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