Structure of PDB 1fcv Chain A

Receptor sequence
>1fcvA (length=324) Species: 7460 (Apis mellifera) [Search protein sequence]
EFNVYWNVPTFMCHKYGLRFEEVSEKYGILQNWMDKFRGEEIAILYDPGM
FPALLKDPNGNVVARNGGVPQLGNLTKHLQVFRDHLINQIPDKSFPGVGV
IDFESWRPIFRQNWASLQPYKKLSVEVVRREHPFWDDQRVEQEAKRRFEK
YGQLFMEETLKAAKRMRPAANWGYYAYPYCYNLTPNQPSAQCEATTMQEN
DKMSWLFESEDVLLPSVYLRWNLTSGERVGLVGGRVKEALRIARQMTTSR
KKVLPYYWYKYQDRRDTDLSRADLEATLRKITDLGADGFIIWGSSDDINT
KAKCLQFREYLNNELGPAVKRIAL
3D structure
PDB1fcv Crystal structure of hyaluronidase, a major allergen of bee venom.
ChainA
Resolution2.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D111 E113 Y184 Y227 W301
Catalytic site (residue number reindexed from 1) D102 E104 Y175 Y218 W292
Enzyme Commision number 3.2.1.35: hyaluronoglucosaminidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GCU A E113 Y184 E104 Y175
BS02 GCU A W301 S303 S304 W292 S294 S295
Gene Ontology
Molecular Function
GO:0004415 hyalurononglucosaminidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006952 defense response
GO:0030214 hyaluronan catabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1fcv, PDBe:1fcv, PDBj:1fcv
PDBsum1fcv
PubMed11080624
UniProtQ08169|HUGA_APIME Hyaluronidase

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