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1GHR

THE THREE-DIMENSIONAL STRUCTURES OF TWO PLANT BETA-GLUCAN ENDOHYDROLASES WITH DISTINCT SUBSTRATE SPECIFICITIES

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0042972molecular_functionlicheninase activity
Functional Information from PROSITE/UniProt
site_idPS00587
Number of Residues14
DetailsGLYCOSYL_HYDROL_F17 Glycosyl hydrolases family 17 signature. VkLVVSESGWPSgG
ChainResidueDetails
AVAL226-GLY239

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:O22317
ChainResidueDetails
AGLU93

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:O22317
ChainResidueDetails
AGLU232

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AASN190

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1aq0
ChainResidueDetails
AGLU280
ALYS283
AGLU288
AGLU232

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aq0
ChainResidueDetails
AGLU288
AGLU232

site_idMCSA1
Number of Residues4
DetailsM-CSA 400
ChainResidueDetails
AGLU232covalent catalysis
AGLU280electrostatic stabiliser
ALYS283electrostatic stabiliser
AGLU288proton shuttle (general acid/base)

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PDB entries from 2024-09-18

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