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1K9E

Crystal structure of a mutated family-67 alpha-D-glucuronidase (E285N) from Bacillus stearothermophilus T-6, complexed with 4-O-methyl-glucuronic acid

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
A0033939molecular_functionxylan alpha-1,2-glucuronosidase activity
A0045493biological_processxylan catabolic process
A0046559molecular_functionalpha-glucuronidase activity
A2000886biological_processglucuronoxylan catabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:14573597
ChainResidueDetails
AASN285

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:14573597
ChainResidueDetails
AASP364
AGLU392

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AGLU158
ALYS281
AARG318
AARG335
ALYS359

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASN201
AGLU386
AGLU510
ATRP540

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Participates in a stacking interactions with the sugar rings of 4-O-MeGlcA => ECO:0000250
ChainResidueDetails
ATRP150
ATRP540

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PDB entries from 2024-05-01

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