Structure of PDB 6iux Chain A

Receptor sequence
>6iuxA (length=358) Species: 9606 (Homo sapiens) [Search protein sequence]
GSEKYVAAMVLSAAGDALGYYNGKWEFLQDGEKIHRQLAQLGGLDALDVG
RWRVSDDTVMHLATAEALVEAGKAPKLTQLYYLLAKHYQDCMEDMDGRAP
GGASVHNAMQLKPGKPNGWRIPFNSHEGGCGAAMRAMCIGLRFPHHSQLD
TLIQVSIESGRMTHHHPTGYLGALASALFTAYAVNSRPPLQWGKGLMELL
PEAKKYIVQSGYFVEENLQHWSYFQTKWENYLKLRGILDGESAPTFPESF
GVKERDQFYTSLSYSGWGGSSGHDAPMIAYDAVLAAGDSWKELAHRAFFH
GGDSDSTAAIAGCWWGVMYGFKGVSPSNYEKLEYRNRLEETARALYSLGS
KEDTVISL
3D structure
PDB6iux Crystal structure of protein
ChainA
Resolution1.195 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 MG A S54 D55 D56 D304 S55 D56 D57 D305
BS02 AR6 A E25 D55 G100 G101 A102 S103 H125 G127 G128 C129 G130 H163 H165 Y263 S269 S270 D302 D304 S305 E26 D56 G101 G102 A103 S104 H126 G128 G129 C130 G131 H164 H166 Y264 S270 S271 D303 D305 S306
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6iux, PDBe:6iux, PDBj:6iux
PDBsum6iux
PubMed
UniProtP54922|ADPRH_HUMAN ADP-ribosylhydrolase ARH1 (Gene Name=ADPRH)

[Back to BioLiP]