1tdh

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spinqualitylabelsall models PDB ID 1tdh Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1tdh, resolution 2.10Å ()
Ligands:
Structural annotation: Resources: InterPro : Ipr010979, Ipr015886, Ipr015371, Ipr015887, Ipr012319 Pfam : PF01149, PF06831, PF09292 SCOP : d1tdha1, d1tdha2, d1tdha3 UniProt : Q96FI4
Functional annotation: Cellular component: nucleus Biological process: DNA repair response to DNA damage stimulus base-excision repair metabolic process Molecular function: oxidized purine base lesion DNA N-glycosylase activity damaged DNA binding zinc ion binding DNA-(apurinic or apyrimidinic site) lyase activity catalytic activity hydrolase activity, acting on glycosyl bonds DNA binding lyase activity hydrolase 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 Crystal structure of human endonuclease VIII-like 1 (NEIL1) 2 About this Structure 3 See Also 4 Reference

Crystal structure of human endonuclease VIII-like 1 (NEIL1)

Template:ABSTRACT PUBMED 15232006

About this Structure

1tdh is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

• DNA glycosylate
• DNA repair protein human endonuclease VIII-like 1 (NEIL1)
• Fpg Nei Protein Family

Reference

• Doublie S, Bandaru V, Bond JP, Wallace SS. The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity. Proc Natl Acad Sci U S A. 2004 Jul 13;101(28):10284-9. Epub 2004 Jul 1. PMID:15232006 doi:10.1073/pnas.0402051101