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1C7S

BETA-N-ACETYLHEXOSAMINIDASE MUTANT D539A COMPLEXED WITH DI-N-ACETYL-BETA-D-GLUCOSAMINE (CHITOBIASE)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004563molecular_functionbeta-N-acetylhexosaminidase activity
A0005764cellular_componentlysosome
A0005975biological_processcarbohydrate metabolic process
A0006032biological_processchitin catabolic process
A0006689biological_processganglioside catabolic process
A0016020cellular_componentmembrane
A0016231molecular_functionbeta-N-acetylglucosaminidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030203biological_processglycosaminoglycan metabolic process
A0030246molecular_functioncarbohydrate binding
A0030247molecular_functionpolysaccharide binding
A0042597cellular_componentperiplasmic space
A0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
Functional Information from PROSITE/UniProt
site_idPS00041
Number of Residues46
DetailsHTH_ARAC_FAMILY_1 Bacterial regulatory proteins, araC family signature. KLepTAkfSgfpagkaveIpVVAEYwQLfrndfLprwYATsgDaKP
ChainResidueDetails
ALYS114-PRO159

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AGLU540

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qba
ChainResidueDetails
AGLU540
AALA539

site_idMCSA1
Number of Residues2
DetailsM-CSA 899
ChainResidueDetails
AALA539electrostatic stabiliser, modifies pKa, steric role
AGLU540proton shuttle (general acid/base)

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PDB entries from 2024-05-01

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