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6EZT

Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase D437A inactive mutant from Vibrio harveyi

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004563molecular_functionbeta-N-acetylhexosaminidase activity
A0005975biological_processcarbohydrate metabolic process
A0016020cellular_componentmembrane
A0016231molecular_functionbeta-N-acetylglucosaminidase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030203biological_processglycosaminoglycan metabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004563molecular_functionbeta-N-acetylhexosaminidase activity
B0005975biological_processcarbohydrate metabolic process
B0016020cellular_componentmembrane
B0016231molecular_functionbeta-N-acetylglucosaminidase activity
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030203biological_processglycosaminoglycan metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue PG4 A 701
ChainResidue
AGLU540
AASN588
ASER590
AARG591
ATYR594
AASN636
AHOH817

site_idAC2
Number of Residues2
Detailsbinding site for residue PEG A 702
ChainResidue
AGLU180
AARG184

site_idAC3
Number of Residues6
Detailsbinding site for residue PEG B 701
ChainResidue
BGLU208
BSER228
BPRO261
BARG266
BASN295
BHOH922

site_idAC4
Number of Residues5
Detailsbinding site for residue PG4 B 702
ChainResidue
BASN588
BSER590
BARG591
BTYR594
BASN636

246031

PDB entries from 2025-12-10

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