Structure of PDB 2nqh Chain A

Receptor sequence

>2nqhA (length=279) Species: 562 (Escherichia coli)

MKYIGAHVSAAGGLANAAIRAAEIDATAFALFTKNQRQWRAAPLTTQTID
EFKAACEKYHYTSAQILPHDSYLINLGHPVTEALEKSRDAFIDEMQRCEQ
LGLSLLNFHPGSHLMQISEEDCLARIAESINIALDKTQGVTAVIENTAGQ
GSNLGFKFEHLAAIIDGVEDKSRVGVCIDTCHAFAAGYDLRTPAECEKTF
ADFARTVGFKYLRGMHLNDAKSTFGSRVDRHHSLGEGNIGHDAFRWIMQD
DRFDGIPLILQTINPDIWAEEIAWLKAQQ

3D structure

• PDB: 2nqh DNA apurinic-apyrimidinic site binding and excision by endonuclease IV.
• Chain: A
• Resolution: 1.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R37 H69 Y72 H109 E145 D179 H182 H216 D229 H231 Q261
• Catalytic site (residue number reindexed from 1): R37 H69 Y72 H109 E145 D179 H182 H216 D229 H231 Q261
• Enzyme Commision number: 3.1.21.2: deoxyribonuclease IV.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ZN	A	H69 H109 E145	H69 H109 E145
BS02	ZN	A	E145 D179 H216 Q261	E145 D179 H216 Q261
BS03	ZN	A	H182 D229 H231	H182 D229 H231
BS04	PO4	A	H69 H109 E145 H182 H231 Q261	H69 H109 E145 H182 H231 Q261

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

External links

• PDB: RCSB:2nqh, PDBe:2nqh, PDBj:2nqh
• PDBsum: 2nqh
• PubMed: 18408731
• UniProt: P0A6C1|END4_ECOLI Endonuclease 4 (Gene Name=nfo)