Structure of PDB 6hh3 Chain A

Receptor sequence
>6hh3A (length=329) Species: 7897 (Latimeria chalumnae) [Search protein sequence]
PMVSLAQVRGALCGALLGDCMGAEFEGSDAVELPDVLEFVRLLEKEKKAG
TLFYTDDTAMTRAVIQSLIAKPDFDEVDMAKRFAEEYKKEPTRGYGAGVV
QVFKKLLSPKYSDVFQPAREQFDGKGSYGNGGAMRVASIALAYPNIQDVI
KFARRSAQLTHASPLGYNGAILQALAVHFALQGELKRDTFLEQLIGEMER
IEGKLPFCSRLKKIKEFLASSNVPKADIVDELGHGIAALESVPTAIYSFL
HCMESDPDIPDLYNNLQRTIIYSISLGGDTDTIATMAGAIAGAYYGMDQV
TPSWKRSCEAIVETEESAVKLYELYCKQL
3D structure
PDB6hh3 (ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition.
ChainA
Resolution1.82 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.143: poly(ADP-ribose) glycohydrolase.
3.2.2.-
3.5.1.-
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 MG A T62 D63 D64 D305 T55 D56 D57 D281
BS02 MG A E33 D303 D305 T306 E26 D279 D281 T282
BS03 A1R A D63 D64 G103 G105 F129 S134 Y135 G136 N137 G138 H168 D303 D305 T306 D56 D57 G96 G98 F122 S127 Y128 G129 N130 G131 H161 D279 D281 T282 PDBbind-CN: -logKd/Ki=6.24,Ki=0.58uM
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004649 poly(ADP-ribose) glycohydrolase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0006281 DNA repair
GO:0060546 negative regulation of necroptotic process
GO:0140290 peptidyl-serine ADP-deribosylation
Cellular Component
GO:0005634 nucleus
GO:0005694 chromosome
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6hh3, PDBe:6hh3, PDBj:6hh3
PDBsum6hh3
PubMed30472116
UniProtH3BCW1|ADPRS_LATCH ADP-ribosylhydrolase ARH3 (Gene Name=adprs)

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