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From Proteopedia

1fn7, resolution 2.60Å ()
Ligands:
Non-Standard Residues:
Related:	1ebm
Structural annotation: Resources: CATH : 1Fn7A02, 1Fn7A01, 1Fn7A03 InterPro : Ipr000445, Ipr012294, Ipr012904, Ipr003265, Ipr011257, Ipr004577 Pfam : PF00633, PF07934, PF00730 SCOP : d1fn7a1, d1fn7a2 UniProt : O15527
Functional annotation: Cellular component: nucleus mitochondrion nucleoplasm intracellular Biological process: response to DNA damage stimulus metabolic process DNA repair base-excision repair Molecular function: catalytic activity hydrolase activity damaged DNA binding protein binding lyase activity endonuclease activity DNA binding DNA-(apurinic or apyrimidinic site) lyase activity hydrolase activity, acting on glycosyl bonds oxidized purine base lesion DNA N-glycosylase 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

COUPLING OF DAMAGE RECOGNITION AND CATALYSIS BY A HUMAN BASE-EXCISION DNA REPAIR PROTEIN

Disease

[OGG1_HUMAN] Defects in OGG1 may be a cause of renal cell carcinoma (RCC) [MIM:144700]. It is a heterogeneous group of sporadic or hereditary carcinoma derived from cells of the proximal renal tubular epithelium. It is subclassified into clear cell renal carcinoma (non-papillary carcinoma), papillary renal cell carcinoma, chromophobe renal cell carcinoma, collecting duct carcinoma with medullary carcinoma of the kidney, and unclassified renal cell carcinoma.

Function

[OGG1_HUMAN] DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion.

About this Structure

1fn7 is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

• DNA glycosylate

Reference

• Norman DP, Bruner SD, Verdine GL. Coupling of substrate recognition and catalysis by a human base-excision DNA repair protein. J Am Chem Soc. 2001 Jan 17;123(2):359-60. PMID:11456534