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5BU9

Crystal structure of Beta-N-acetylhexosaminidase from Beutenbergia cavernae DSM 12333

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004563molecular_functionbeta-N-acetylhexosaminidase activity
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004563molecular_functionbeta-N-acetylhexosaminidase activity
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue GOL A 501
ChainResidue
AASP147
ALEU198
AARG222
ALYS252
AHIS253
AMSE297
AASP336
AGOL502

site_idAC2
Number of Residues3
Detailsbinding site for residue GOL A 502
ChainResidue
AGOL501
AHOH652
AVAL153

site_idAC3
Number of Residues9
Detailsbinding site for residue GOL B 501
ChainResidue
BASP147
BLEU198
BARG222
BLYS252
BHIS253
BMSE297
BASP336
BLEU365
BHOH602

site_idAC4
Number of Residues3
Detailsbinding site for residue GOL B 502
ChainResidue
BASN263
BASP265
BHOH695

Functional Information from PROSITE/UniProt
site_idPS00775
Number of Residues18
DetailsGLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. LLRgQlgfdGVVVTDdvS
ChainResidueDetails
ALEU322-SER339

223166

PDB entries from 2024-07-31

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