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6JEA

crystal structure of a beta-N-acetylhexosaminidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004563molecular_functionbeta-N-acetylhexosaminidase activity
A0005975biological_processcarbohydrate metabolic process
A0016020cellular_componentmembrane
A0016231molecular_functionbeta-N-acetylglucosaminidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030203biological_processglycosaminoglycan metabolic process
A0032428molecular_functionbeta-N-acetylgalactosaminidase activity
A0046872molecular_functionmetal ion binding
A0052781biological_processchitobiose catabolic process
A0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:30846208, ECO:0007744|PDB:6JE8, ECO:0007744|PDB:6JEA, ECO:0007744|PDB:6JEB
ChainResidueDetails
AASP151
AHIS214

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:30846208, ECO:0007744|PDB:6JEB
ChainResidueDetails
AGLU279

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:30846208, ECO:0007744|PDB:6JEA
ChainResidueDetails
AARG122
AASP278
ATRP345
ATYR373
ATRP421

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:30846208, ECO:0007744|PDB:6JE8, ECO:0007744|PDB:6JEA, ECO:0007744|PDB:6JEB
ChainResidueDetails
ACYS227
ACYS247
ACYS288
ACYS291

225158

PDB entries from 2024-09-18

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