Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
PB Lead (II) ion
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1HD7   PDBj   RCSB PDB   PDBe
Header : DNA REPAIR
Title : A Second Divalent Metal Ion in the Active Site of a New Crystal Form of Human Apurinic/Apyridinimic Endonuclease, Ape1, and its Implications for the Catalytic Mechanism
Release Data : 2001-02-16
Compound :
mol_id molecule chains synonym
1 DNA-(APURINIC OR APYRIMIDINIC SITE) LYASE A AP ENDONUCLEASE 1, HAP1, REF1, APE1
ec: 4.2.99.18
Source :
mol_id organism_scientific organism_common expression_system
1 HOMO SAPIENS  (taxid:9606) HUMAN ESCHERICHIA COLI  (taxid:469008)
tissue: ALL
cell: ALL
organelle: NUCLEUS
expression_system_strain: BL21(DE3)
expression_system_plasmid: PET11D
expression_system_gene: APE1
Authors : Beernink, P.T., Segelke, B.W., Rupp, B.
Keywords : DNA REPAIR, ENDONUCLEASE, APE1, HAP1, REF-1
Exp. method : X-RAY DIFFRACTION ( 1.95 Å )
Citation :

Two Divalent Metal Ions in the Active Site of a New Crystal Form of Human Apurinic/Apyrimidinic Endonuclease, Ape1: Implications for the Catalytic Mechanism

Beernink, P.T.,Segelke, B.W.,Hadi, M.Z.  et al.
(2001)  J.Mol.Biol.  307 : 1023

PubMed: 11286553
DOI: 10.1006/JMBI.2001.4529

Chain : A
UniProt : P27695 (APEX1_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates. 3.1.11.2 PubMed:11286553, PubMed:15380100, PubMed:19123919, PubMed:21762700, PubMed:9804799
-