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1REO

L-amino acid oxidase from Agkistrodon halys pallas

Summary for 1REO
Entry DOI10.2210/pdb1reo/pdb
DescriptorAHPLAAO, 2-acetamido-2-deoxy-beta-D-glucopyranose, CITRIC ACID, ... (5 entities in total)
Functional Keywordsl-amino acid oxidase, oxidoreductase
Biological sourceGloydius halys (halys viper)
Cellular locationSecreted: Q6STF1
Total number of polymer chains1
Total formula weight56627.29
Authors
Zhang, H.,Teng, M.,Niu, L.,Wang, Y.,Wang, Y.,Liu, Q.,Huang, Q.,Hao, Q.,Dong, Y.,Liu, P. (deposition date: 2003-11-07, release date: 2004-05-04, Last modification date: 2024-10-30)
Primary citationZhang, 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: 15103157
DOI: 10.1107/S0907444904000046
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.31 Å)
Structure validation

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数据于2024-10-30公开中

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