1FCU
CRYSTAL STRUCTURE (TRIGONAL) OF BEE VENOM HYALURONIDASE
Summary for 1FCU
Entry DOI | 10.2210/pdb1fcu/pdb |
Related | 1FCQ 1FCV |
Descriptor | HYALURONOGLUCOSAMINIDASE (2 entities in total) |
Functional Keywords | 7 stranded (beta/alpha) tim barrel, allergen, glycosidase family 56, hydrolase |
Biological source | Apis mellifera (honey bee) |
Cellular location | Secreted: Q08169 |
Total number of polymer chains | 1 |
Total formula weight | 40901.33 |
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 citation | Markovic-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: 11080624DOI: 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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