Structure of PDB 4zux Chain j Binding Site BS01

Receptor Information
>4zux Chain j (length=447) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AMSICPHIQQVFQNEKSKDGVLKTCNAARYILNHSVPKEKFLNTMKCGCH
EINSGATFMCLQCGFCGCWNHSHFLSHSKQIGHIFGINSNNGLLFCFKCE
DYIGNIDLINDAILAKYWDDVCTKTMVPSMERRDGLSGLINMGSTAFMSS
ILQCLIHNPYFIRHSMSQIHSNNCKVRSPDKCFSCALDKIVHELYGALNT
STNRQTGFIYLLTCAWKINQNLAGYSQQDAHEFWQFIINQIHQSYVLDLP
NNNKQCECIVHTVFEGSLESSIVCPGCQNNSKTTIDPFLDLSLDIKDKKK
LYECLDSFHKKEQLKDFNYHCGECNSTQDAIKQLGIHKLPSVLVLQLKRF
EHLLNGSNRKLDDFIEFPTYLNMKNYCSTGKVPDIIYELIGIVSHKGTVN
EGHYIAFCKISGGQWFKFNDSMVSSISQEEVLKEQAYLLFYTIRQVN
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain4zux Chain j Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4zux Structural basis for histone H2B deubiquitination by the SAGA DUB module.
Resolution3.82 Å
Binding residue
(original residue number in PDB)		C289 C292 C336 C339
Binding residue
(residue number reindexed from 1)		C274 C277 C321 C324
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) H427 N443
Catalytic site (residue number reindexed from 1) H403 N419
Enzyme Commision number 3.4.19.12: ubiquitinyl hydrolase 1.
Gene Ontology
Molecular Function
GO:0004843 cysteine-type deubiquitinase activity
GO:0005515 protein binding
GO:0008234 cysteine-type peptidase activity
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
GO:0060090 molecular adaptor activity
Biological Process
GO:0006357 regulation of transcription by RNA polymerase II
GO:0006508 proteolysis
GO:0008380 RNA splicing
GO:0016579 protein deubiquitination
Cellular Component
GO:0000124 SAGA complex
GO:0005634 nucleus
GO:0046695 SLIK (SAGA-like) complex
GO:0071819 DUBm complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4zux, PDBe:4zux, PDBj:4zux
PDBsum4zux
PubMed26912860
UniProtP50102|UBP8_YEAST Ubiquitin carboxyl-terminal hydrolase 8 (Gene Name=UBP8)

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