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1FCQ

CRYSTAL STRUCTURE (MONOCLINIC) OF BEE VENOM HYALURONIDASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004415molecular_functionhyalurononglucosaminidase activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0006952biological_processdefense response
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030214biological_processhyaluronan catabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:11080624
ChainResidueDetails
AGLU113

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN83

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10998264
ChainResidueDetails
AASN231

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11080624, Tews1997
ChainResidueDetails
AASP111

site_idMCSA1
Number of Residues5
DetailsM-CSA 616
ChainResidueDetails
AASP111electrostatic stabiliser, modifies pKa, steric role
AGLU113activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
ATYR184steric role
ATYR227electrostatic stabiliser, steric role, transition state stabiliser
ATRP301steric role

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PDB entries from 2024-10-30

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