Structure of PDB 2voa Chain B

Receptor sequence
>2voaB (length=257) Species: 2234 (Archaeoglobus fulgidus) [Search protein sequence]
MLKIATFNVNSIRSRLHIVIPWLKENKPDILCMQETKVENRKFPEADFHR
IGYHVVFSGSKGRNGVAIASLEEPEDVSFGLDSEPKDEDRLIRAKIAGID
VINTYVPQGFKIDSEKYQYKLQWLERLYHYLQKTVDFRSFAVWCGDMNVA
PEPIDVHSPDKLKNHVCFHEDARRAYKKILELGFVDVLRKIHPNERIYTF
YDYRVKGAIERGLGWRGDAILATPPLAERCVDCYADIKPRLAEKPSDHLP
LVAVFDV
3D structure
PDB2voa Structure and Function of the Abasic Site Specificity Pocket of an Ap Endonuclease from Archaeoglobus Fulgidus.
ChainB
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N8 N10 E35 Y105 D146 N148 D218 D247 H248
Catalytic site (residue number reindexed from 1) N8 N10 E35 Y105 D146 N148 D218 D247 H248
Enzyme Commision number 4.2.99.18: DNA-(apurinic or apyrimidinic site) lyase.
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 dna B Q108 F110 R204 Q108 F110 R204
BS02 dna B S11 S14 R15 G62 Y203 R204 S11 S14 R15 G62 Y203 R204
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0003824 catalytic activity
GO:0004518 nuclease activity
GO:0004519 endonuclease activity
GO:0008311 double-stranded DNA 3'-5' DNA exonuclease activity
GO:0046872 metal ion binding
Biological Process
GO:0006281 DNA repair

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Molecular Function
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Biological Process
External links
PDB RCSB:2voa, PDBe:2voa, PDBj:2voa
PDBsum2voa
PubMed19015049
UniProtO29675

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