Structure of PDB 4l2h Chain A

Receptor sequence
>4l2hA (length=436) Species: 5911 (Tetrahymena thermophila) [Search protein sequence]
DYQFPLPQKNSELWIIQKKTLQDLSSGKQKLDSFQSLESILEILRDSKNQ
NDEKYFNLKAVFEQLDKEEQTYFLEQFIPKICQLVLKIKKKQLKNQIPKE
SKIYEAAFSREEISYYVSCMFLCILKDQDRKIYKDFRLIYLKDLVQQINI
RRQEKIKCFYEYLKQALDFSEKESKEVVIFQRINCGQLEDYENWVDKLKA
IKLKNVQLTDDKLIEDFPGTLQVDFANCDIGGGILGNGLVQEQIRFCVCP
EMLVSLLVFDQSMEANEVIIMKGIKQYSDYQGYSNSFRFVKMGNSKIQKQ
KRNNPQTILAIDALCFNSSDNQFSEVNVSRELNKSYMGFKQEDQLKTIST
GKWGCGAFLGVFDLKFAIQWIASSRSNKKMIICTFQDEQTTKQIQQVFDL
YKQKNASIFLKLVMDYPNSKYMEDYTLLEYLIELGK
3D structure
PDB4l2h Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities.
ChainA
Resolution1.46 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.143: poly(ADP-ribose) glycohydrolase.
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 AR6 A R164 G249 N250 G251 L252 V253 Q256 S297 R151 G236 N237 G238 L239 V240 Q243 S284
BS02 AR6 A L226 I227 E228 F238 N240 V253 Q254 E255 Q256 Y296 K365 G367 G369 A370 F371 F398 L213 I214 E215 F225 N227 V240 Q241 E242 Q243 Y283 K352 G354 G356 A357 F358 F385
Gene Ontology
Molecular Function
GO:0004649 poly(ADP-ribose) glycohydrolase activity
GO:0016787 hydrolase activity
GO:0072570 ADP-D-ribose binding
GO:0140292 ADP-ribosylserine hydrolase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006282 regulation of DNA repair
GO:0009225 nucleotide-sugar metabolic process
GO:1990966 ATP generation from poly-ADP-D-ribose
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4l2h, PDBe:4l2h, PDBj:4l2h
PDBsum4l2h
PubMed23917065
UniProtI6L8L7

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