Brand  (β version)

PDB ID: 1BIX

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Ligands
Code Name Style Show Link
PT Platinum (II) ion PoSSuM
SM Samarium (III) ion PoSSuM
Non-standard Residues
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Structure summary

Code : 1BIX   PDBj   RCSB PDB   PDBe
Header : DNA REPAIR
Title : THE CRYSTAL STRUCTURE OF THE HUMAN DNA REPAIR ENDONUCLEASE HAP1 SUGGESTS THE RECOGNITION OF EXTRA-HELICAL DEOXYRIBOSE AT DNA ABASIC SITES
Release Data : 1999-06-22
Compound :
mol_id molecule chains
1 AP ENDONUCLEASE 1 A
ec: 4.2.99.18
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli BL21(DE3)  (taxid:469008)
expression_system_strain: BL21 (DE3)
Authors : Gorman, M.A., Morera, S., Rothwell, D.G., De La Fortelle, E., Mol, C.D., Tainer, J.A., Hickson, I.D., Freemont, P.S.
Keywords : DNA REPAIR, ENDONUCLEASE, HAP1, REF-1, ABASIC SITE RECOGNITION
Exp. method : X-RAY DIFFRACTION ( 2.2 Å )
Citation :

The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites.

Gorman, M.A.,Morera, S.,Rothwell, D.G.  et al.
(1997)  EMBO J.  16 : 6548 - 6558

PubMed: 9351835
DOI: 10.1093/emboj/16.21.6548

Crystal Structure of the Human DNA Repair Enzyme Ap Endonuclease 1

Gorman, M.A.
(1998)  Thesis, The Open University 

Reaction

Chain : A
UniProt : P27695 (APEX1_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
a deoxyribonucleotide-2'-deoxyribose-5'-monophosphate-DNA + H2O = a 5'-end 2'-deoxyribose-5'-monophosphate-DNA + a 3'-end 2'- deoxyribonucleotide-DNA + H(+) - PubMed:15380100, PubMed:24079850, PubMed:8995436
left-to-right PubMed:19934257
Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates. 3.1.11.2 PubMed:11832948
-
a 3'-end 2'-deoxyribonucleotide-3'-phosphoglycolate-DNA + H2O = 2-phosphoglycolate + a 3'-end 2'-deoxyribonucleotide-DNA + H(+) - PubMed:7516064
left-to-right
a 3'-end 2'-deoxyribonucleotide-8-oxoguanine-DNA + H2O = 8- oxo-dGMP + a 3'-end 2'-deoxyribonucleotide-DNA + H(+) - PubMed:15831793
left-to-right
Cofactor: Evidence: Note:
Mn(2+) ECO:0000269 | PubMed:11286553
ECO:0000269 | PubMed:19123919
ECO:0000269 | PubMed:21762700
ECO:0000269 | PubMed:24079850
ECO:0000269 | PubMed:9804799
ECO:0000269 | PubMed:11286553
ECO:0000269 | PubMed:19123919
ECO:0000269 | PubMed:21762700
ECO:0000269 | PubMed:24079850
ECO:0000269 | PubMed:9804799
Probably binds two magnesium or manganese ions per subunit.