Structure of PDB 6g2a Chain A

Receptor sequence
>6g2aA (length=361) Species: 9606 (Homo sapiens) [Search protein sequence]
HHGGMEKYVAAMVLSAAGDALGYYNGKWEFLQDGEKIHRQLAQLGGLDAL
DVGRWRVSDDTVMHLATAEALVEAGKAPKLTQLYYLLAKHYQDCMEDMDG
RAPGGASVHNAMQLKPGKPNGWRIPFNSHEGGCGAAMRAMCIGLRFPHHS
QLDTLIQVSIESGRMTHHHPTGYLGALASALFTAYAVNSRPPLQWGKGLM
ELLPEAKKYIVQSGYFVEENLQHWSYFQTKWENYLKLRGILDGESAPTFP
ESFGVKERDQFYTSLSYSGWGGSSGHDAPMIAYDAVLAAGDSWKELAHRA
FFHGGDSDSTAAIAGCWWGVMYGFKGVSPSNYEKLEYRNRLEETARALYS
LGSKEDTVISL
3D structure
PDB6g2a (ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition.
ChainA
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.2.19: [protein ADP-ribosylarginine] hydrolase.
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 A3R A D55 G100 G101 A102 S103 H125 G127 G128 C129 G130 H163 H165 T167 Y263 S269 S270 D304 S305 D59 G104 G105 A106 S107 H129 G131 G132 C133 G134 H167 H169 T171 Y267 S273 S274 D308 S309 PDBbind-CN: -logKd/Ki=3.79,IC50=164uM
BS02 MG A S54 D55 D56 D304 S58 D59 D60 D308
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003875 ADP-ribosylarginine hydrolase activity
GO:0005515 protein binding
GO:0016787 hydrolase activity
GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds
GO:0030955 potassium ion binding
GO:0046872 metal ion binding
Biological Process
GO:0036211 protein modification process
GO:0051725 protein de-ADP-ribosylation
Cellular Component
GO:0005615 extracellular space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6g2a, PDBe:6g2a, PDBj:6g2a
PDBsum6g2a
PubMed30472116
UniProtP54922|ADPRH_HUMAN ADP-ribosylhydrolase ARH1 (Gene Name=ADPRH)

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