Structure of PDB 5udh Chain B

Receptor sequence
>5udhB (length=381) Species: 9606 (Homo sapiens) [Search protein sequence]
DYRYEVLTAEQILQHMVECIREVNEVIQNPATITRILLSHFNWDKEKLME
RYFDGMPCQICYLNYPNSYFTGLECGHKFCMQCWSEYLTTKIMEEGMGQT
ISCPAHGCDILVDDNTVMRLITDSKVKLKYQHLITNSFVECNRLLKWCPA
PDCHHVVKVQYPDAKPVRCKCGRQFCFNCGENWHDPVKCKWLKKWIKKCD
NTKECPKCHVTIEKDGGCNHMVCRNQNCKAEFCWVCLGPWEPHGSAWYNC
NRAALQRYLFYCNRYMNHMQSLRFEHKLYAQVKQKFLKKAVDVLCQCRAT
LMYTYVFAFYLKKNNQSIIFENNQADLENATEVLSGYLERDISQDSLQDI
KQKVQDKYRYCESRRRVLLQHVHEGYEKDLW
3D structure
PDB5udh Structural Studies of HHARI/UbcH7Ub Reveal Unique E2Ub Conformational Restriction by RBR RING1.
ChainB
Resolution3.24 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.2.31: RBR-type E3 ubiquitin transferase.
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 ZN B C344 C347 C362 C367 C205 C208 C223 C228
BS02 ZN B C372 C375 H382 C389 C233 C236 H243 C250
BS03 ZN B C276 C281 C297 C299 C148 C153 C169 C171
BS04 ZN B C304 C307 H312 C317 C176 C179 H184 C189
BS05 ZN B C186 C189 C208 C211 C58 C61 C80 C83
BS06 ZN B C203 H205 C231 C236 C75 H77 C103 C108
Gene Ontology
Molecular Function
GO:0004842 ubiquitin-protein transferase activity
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
Biological Process
GO:0016567 protein ubiquitination

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Molecular Function
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Biological Process
External links
PDB RCSB:5udh, PDBe:5udh, PDBj:5udh
PDBsum5udh
PubMed28552575
UniProtQ9Y4X5|ARI1_HUMAN E3 ubiquitin-protein ligase ARIH1 (Gene Name=ARIH1)

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