Structure of PDB 3w52 Chain A

Receptor sequence
>3w52A (length=256) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
WGKEGHEIICKIAQTRLDETAAKAVKELLPESAEGDLSSLCLWADRVKFR
YHWSSPLHYINTPDACSYQYNRDCKDESGEKGRCVAGAIYNYTTQLLSYK
QYNLTEALLFVSHFMGDIHQPLHVSYASDKGGNTIEVHWYTRKANLHHIW
DSNIIETAEADLYNSALEGMVDALKKNITTEWADQVKRWETCTKKTACPD
IYASEGIQAACDWAYKGVTEGDTLEDEYFYSRLPIVYQRLAQGGVRLAAT
LNRIFG
3D structure
PDB3w52 Mechanistic insights to catalysis by a zinc-dependent bi-functional nuclease from Arabidopsis thaliana
ChainA
Resolution1.76 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W1 H6 D45 K48 H58 H120 D124 H130 H154 D158
Catalytic site (residue number reindexed from 1) W1 H6 D45 K48 H58 H113 D117 H123 H147 D151
Enzyme Commision number 3.1.30.1: Aspergillus nuclease S1.
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 ADE A Y59 K137 H154 Y59 K130 H147
BS02 ZN A D45 H58 H120 D124 D45 H58 H113 D117
BS03 ZN A H130 H154 D158 H123 H147 D151
BS04 ZN A W1 H6 D124 W1 H6 D117
Gene Ontology
Molecular Function
GO:0000014 single-stranded DNA endodeoxyribonuclease activity
GO:0003676 nucleic acid binding
GO:0004519 endonuclease activity
GO:0004521 RNA endonuclease activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0043765 T/G mismatch-specific endonuclease activity
GO:0046872 metal ion binding
GO:1990238 double-stranded DNA endonuclease activity
Biological Process
GO:0006308 DNA catabolic process

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Molecular Function

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Biological Process
External links
PDB RCSB:3w52, PDBe:3w52, PDBj:3w52
PDBsum3w52
PubMed
UniProtQ9C9G4|ENDO2_ARATH Endonuclease 2 (Gene Name=ENDO2)

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