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1FCU

CRYSTAL STRUCTURE (TRIGONAL) OF BEE VENOM HYALURONIDASE

Summary for 1FCU
Entry DOI10.2210/pdb1fcu/pdb
Related1FCQ 1FCV
DescriptorHYALURONOGLUCOSAMINIDASE (2 entities in total)
Functional Keywords7 stranded (beta/alpha) tim barrel, allergen, glycosidase family 56, hydrolase
Biological sourceApis mellifera (honey bee)
Cellular locationSecreted: Q08169
Total number of polymer chains1
Total formula weight40901.33
Authors
Markovic-Housley, Z.,Miglierini, G.,Soldatova, L.,Rizkallah, P.J.,Mueller, U.,Schirmer, T. (deposition date: 2000-07-19, release date: 2001-10-01, Last modification date: 2024-10-09)
Primary citationMarkovic-Housley, Z.,Miglierini, G.,Soldatova, L.,Rizkallah, P.J.,Muller, U.,Schirmer, T.
Crystal structure of hyaluronidase, a major allergen of bee venom.
Structure Fold.Des., 8:1025-1035, 2000
Cited by
PubMed Abstract: Hyaluronic acid (HA) is the most abundant glycosaminoglycan of vertebrate extracellular spaces and is specifically degraded by a beta-1,4 glycosidase. Bee venom hyaluronidase (Hya) shares 30% sequence identity with human hyaluronidases, which are involved in fertilization and the turnover of HA. On the basis of sequence similarity, mammalian enzymes and Hya are assigned to glycosidase family 56 for which no structure has been reported yet.
PubMed: 11080624
DOI: 10.1016/S0969-2126(00)00511-6
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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