1REO
L-amino acid oxidase from Agkistrodon halys pallas
Summary for 1REO
Entry DOI | 10.2210/pdb1reo/pdb |
Descriptor | AHPLAAO, 2-acetamido-2-deoxy-beta-D-glucopyranose, CITRIC ACID, ... (5 entities in total) |
Functional Keywords | l-amino acid oxidase, oxidoreductase |
Biological source | Gloydius halys (halys viper) |
Cellular location | Secreted: Q6STF1 |
Total number of polymer chains | 1 |
Total formula weight | 56627.29 |
Authors | |
Primary citation | Zhang, H.,Teng, M.,Niu, L.,Wang, Y.,Wang, Y.,Liu, Q.,Huang, Q.,Hao, Q.,Dong, Y.,Liu, P. Purification, partial characterization, crystallization and structural determination of AHP-LAAO, a novel L-amino-acid oxidase with cell apoptosis-inducing activity from Agkistrodon halys pallas venom. Acta Crystallogr.,Sect.D, 60:974-977, 2004 Cited by PubMed Abstract: A snake-venom protein named AHP-LAAO has been purified from Agkistrodon halys pallas venom using four-stage chromatography. AHP-LAAO is a novel member of the snake-venom L-amino-acid oxidase family. Its amino-acid sequence shows high homology to other members of this family. For L-leucine, the values of k(cat) and K(M) are 31.1 s(-1) and 0.25 mM, respectively. The molecular weight of AHP-LAAO is about 60.7 kDa as determined by MALDI-TOF mass spectrometry. AHP-LAAO can also induce apoptosis of cultured Hela cells. Two sets of diffraction data with similar resolution limits (about 2.5 A) were collected independently at MacCHESS (Cornell High Energy Synchrotron Source, USA) and IHEP (Institute of High Energy Physics, Beijing, China). The crystals belong to space group I2(1)3, with unit-cell parameter a = 169.31 A, corresponding to one molecule in the asymmetric unit and a volume-to-weight ratio of 3.33 A(3) Da(-1). The final structural model is similar to that of L-amino-acid oxidase from Calloselasma rhodostoma venom. PubMed: 15103157DOI: 10.1107/S0907444904000046 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.31 Å) |
Structure validation
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