1a36

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Revision as of 12:58, 28 April 2011

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spinqualitylabelsall models PDB ID 1a36 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1a36, resolution 2.80Å ()
Activity:	DNA topoisomerase, with EC number 5.99.1.2
Structural annotation: Resources: CATH : 1A36A03, 1A36A02, 1A36A01, 1A36A04 InterPro : Ipr011010, Ipr009054, Ipr013500, Ipr013499, Ipr001631, Ipr013030, Ipr008336, Ipr014727, Ipr014711 Pfam : PF02919, PF01028 SCOP : d1a36a2, d1a36a1, d1a36a3 UniProt : P11387
Functional annotation: Cellular component: nucleolus perikaryon chromosome nucleoplasm cytoplasm nucleus Biological process: DNA unwinding during replication response to drug embryonic cleavage phosphorylation DNA topological change programmed cell death DNA replication Molecular function: DNA topoisomerase activity DNA topoisomerase (ATP-hydrolyzing) activity DNA binding chromatin binding protein binding isomerase activity DNA topoisomerase type I activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Contents 1 TOPOISOMERASE I/DNA COMPLEX 2 About this Structure 3 See Also 4 Reference

TOPOISOMERASE I/DNA COMPLEX

Template:ABSTRACT PUBMED 9488652

About this Structure

1a36 is a 3 chain structure of Topoisomerase with sequence from Homo sapiens. The January 2006 RCSB PDB Molecule of the Month feature on Topoisomerases by David S. Goodsell is 10.2210/rcsb_pdb/mom_2006_1. Full crystallographic information is available from OCA.

See Also

• Topoisomerase

Reference

• Stewart L, Redinbo MR, Qiu X, Hol WG, Champoux JJ. A model for the mechanism of human topoisomerase I. Science. 1998 Mar 6;279(5356):1534-41. PMID:9488652
• Redinbo MR, Stewart L, Champoux JJ, Hol WG. Structural flexibility in human topoisomerase I revealed in multiple non-isomorphous crystal structures. J Mol Biol. 1999 Sep 24;292(3):685-96. PMID:10497031 doi:10.1006/jmbi.1999.3065