Structure of PDB 4k1g Chain B

Receptor sequence
>4k1gB (length=279) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MKYIGAHVSAAGGLANAAIRAAEIDATAFALFTKNQRQWRAAPLTTQTID
EFKAACEKYHYTSAQILPADSYLINLGHPVTEALEKSRDAFIDEMQRCEQ
LGLSLLNFHPGSHLMQISEEDCLARIAESINIALDKTQGVTAVIENTAGQ
GSNLGFKFEHLAAIIDGVEDKSRVGVCIDTCHAFAAGYDLRTPAECEKTF
ADFARTVGFKYLRGMHLNDAKSTFGSRVDRHHSLGEGNIGHDAFRWIMQD
DRFDGIPLILETINPDIWAEEIAWLKAQQ
3D structure
PDB4k1g Insight into mechanisms of 3'-5' exonuclease activity and removal of bulky 8,5'-cyclopurine adducts by apurinic/apyrimidinic endonucleases.
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) R37 A69 Y72 H109 E145 D179 H182 H216 D229 H231 E261
Catalytic site (residue number reindexed from 1) R37 A69 Y72 H109 E145 D179 H182 H216 D229 H231 E261
Enzyme Commision number 3.1.21.2: deoxyribonuclease IV.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0003906 DNA-(apurinic or apyrimidinic site) endonuclease activity
GO:0004519 endonuclease activity
GO:0008081 phosphoric diester hydrolase activity
GO:0008270 zinc ion binding
GO:0008296 3'-5'-DNA exonuclease activity
GO:0008833 deoxyribonuclease IV (phage-T4-induced) activity
GO:0016791 phosphatase activity
GO:0046872 metal ion binding
Biological Process
GO:0006281 DNA repair
GO:0006284 base-excision repair
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4k1g, PDBe:4k1g, PDBj:4k1g
PDBsum4k1g
PubMed23898172
UniProtP0A6C1|END4_ECOLI Endonuclease 4 (Gene Name=nfo)

[Back to BioLiP]