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6VE1

Crystal structure of endo-beta-N-acetylglucosaminidase H at high pH

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
A0033925molecular_functionmannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0033925molecular_functionmannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005576cellular_componentextracellular region
C0005975biological_processcarbohydrate metabolic process
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0033925molecular_functionmannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005576cellular_componentextracellular region
D0005975biological_processcarbohydrate metabolic process
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0033925molecular_functionmannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG A 301
ChainResidue
AASP187
ASER189
AALA209
AHOH522
BASP239

site_idAC2
Number of Residues2
Detailsbinding site for residue MG A 302
ChainResidue
AASP190
AHOH498

site_idAC3
Number of Residues5
Detailsbinding site for residue MG B 301
ChainResidue
BLEU210
BGLN214
BHOH647
BASP190
BPHE192

site_idAC4
Number of Residues3
Detailsbinding site for residue MG C 301
ChainResidue
CASN22
CALA49
CASN66

site_idAC5
Number of Residues5
Detailsbinding site for residue MG C 302
ChainResidue
CTYR32
CASP251
CGLY252
CGLY253
CARG273

site_idAC6
Number of Residues5
Detailsbinding site for residue MG D 301
ChainResidue
DASN173
DASN197
DGLN204
DPRO206
DHOH449

Functional Information from PROSITE/UniProt
site_idPS01095
Number of Residues9
DetailsGH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. LDGVDFDdE
ChainResidueDetails
ALEU128-GLU136

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01258, ECO:0000305|PubMed:10595536
ChainResidueDetails
AGLU136
BGLU136
CGLU136
DGLU136

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PDB entries from 2024-07-24

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