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6JZ7

b-glucuronidase from Ruminococcus gnavus in complex with N1-substituted uronic isofagomine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004565molecular_functionbeta-galactosidase activity
A0004566molecular_functionbeta-glucuronidase activity
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0019391biological_processglucuronoside catabolic process
A0030246molecular_functioncarbohydrate binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004565molecular_functionbeta-galactosidase activity
B0004566molecular_functionbeta-glucuronidase activity
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0019391biological_processglucuronoside catabolic process
B0030246molecular_functioncarbohydrate binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue CKU A 701
ChainResidue
AASP167
AHOH831
AHOH911
AHOH1120
AHIS335
ATYR474
ATYR478
AGLU512
ATRP557
AARG570
AASN574
ALYS576

site_idAC2
Number of Residues14
Detailsbinding site for residue CKU B 701
ChainResidue
BASP167
BHIS335
BASN472
BTYR474
BTYR478
BGLU512
BTRP557
BARG570
BASN574
BLYS576
BHOH818
BHOH924
BHOH950
BHOH1247

Functional Information from PROSITE/UniProt
site_idPS00719
Number of Residues26
DetailsGLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NcFRTSHYPyaeeWYqfaDeeGFLII
ChainResidueDetails
AASN329-ILE354

222624

PDB entries from 2024-07-17

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