Structure of PDB 5udh Chain B Binding Site BS02
Receptor Information
>5udh Chain B (length=381) Species:
9606
(Homo sapiens) [
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DYRYEVLTAEQILQHMVECIREVNEVIQNPATITRILLSHFNWDKEKLME
RYFDGMPCQICYLNYPNSYFTGLECGHKFCMQCWSEYLTTKIMEEGMGQT
ISCPAHGCDILVDDNTVMRLITDSKVKLKYQHLITNSFVECNRLLKWCPA
PDCHHVVKVQYPDAKPVRCKCGRQFCFNCGENWHDPVKCKWLKKWIKKCD
NTKECPKCHVTIEKDGGCNHMVCRNQNCKAEFCWVCLGPWEPHGSAWYNC
NRAALQRYLFYCNRYMNHMQSLRFEHKLYAQVKQKFLKKAVDVLCQCRAT
LMYTYVFAFYLKKNNQSIIFENNQADLENATEVLSGYLERDISQDSLQDI
KQKVQDKYRYCESRRRVLLQHVHEGYEKDLW
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
5udh Chain B Residue 602 [
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Receptor-Ligand Complex Structure
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PDB
5udh
Structural Studies of HHARI/UbcH7Ub Reveal Unique E2Ub Conformational Restriction by RBR RING1.
Resolution
3.24 Å
Binding residue
(original residue number in PDB)
C372 C375 H382 C389
Binding residue
(residue number reindexed from 1)
C233 C236 H243 C250
Annotation score
4
Enzymatic activity
Enzyme Commision number
2.3.2.31
: RBR-type E3 ubiquitin transferase.
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
PDBsum
5udh
PubMed
28552575
UniProt
Q9Y4X5
|ARI1_HUMAN E3 ubiquitin-protein ligase ARIH1 (Gene Name=ARIH1)
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