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3C7F

Crystal structure of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase from bacillus subtilis in complex with xylotriose.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
A0045493biological_processxylan catabolic process
A0046556molecular_functionalpha-L-arabinofuranosidase activity
A0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:18980579
ChainResidueDetails
AASP24

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:18980579
ChainResidueDetails
AGLU225

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:18980579
ChainResidueDetails
AASN383
AGLN384
AASP480
AASN288
AGLU359
AGLU361

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for catalytic activity, responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate => ECO:0000305|PubMed:18980579
ChainResidueDetails
AASP163

219869

PDB entries from 2024-05-15

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