Structure of PDB 3hfw Chain A

Receptor sequence
>3hfwA (length=357) Species: 9606 (Homo sapiens) [Search protein sequence]
MEKYVAAMVLSAAGDALGYYNGKWEFLQDGEKIHRQLAQLGGLDALDVGR
WRVSDDTVMHLATAEALVEAGKAPKLTQLYYLLAKHYQDCMEDMDGRAPG
GASVHNAMQLKPGKPNGWRIPFNSHEGGCGAAMRAMCIGLRFPHHSQLDT
LIQVSIESGRMTHHHPTGYLGALASALFTAYAVNSRPPLQWGKGLMELLP
EAKKYIVQSGYFVEENLQHWSYFQTKWENYLKLRGILDGESAPTFPESFG
VKERDQFYTSLSYSGWGGSSGHDAPMIAYDAVLAAGDSWKELAHRAFFHG
GDSDSTAAIAGCWWGVMYGFKGVSPSNYEKLEYRNRLEETARALYSLGSK
EDTVISL
3D structure
PDB3hfw Crystal Structure of human ADP-ribosylhydrolase 1
ChainA
Resolution1.92 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 ADP A G100 G101 A102 S103 H125 G127 G128 G130 H163 Y263 S264 S269 S270 G100 G101 A102 S103 H125 G127 G128 G130 H163 Y263 S264 S269 S270
BS02 MG A S54 D55 D56 D304 S54 D55 D56 D304
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:3hfw, PDBe:3hfw, PDBj:3hfw
PDBsum3hfw
PubMed
UniProtP54922|ADPRH_HUMAN ADP-ribosylhydrolase ARH1 (Gene Name=ADPRH)

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