Structure of PDB 4fk5 Chain A Binding Site BS04

Receptor Information
>4fk5 Chain A (length=437) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AAMSICPHIQQVFQNEKSKDGVLKTCNAARYILNHSVPKEKFLNTMKCGT
CHEINSGATFMCLQCGFCGCWNHSHFLSHSKQIGHIFGINSNNGLLFCFK
CEDYIGNIDLINDAILAKYWDDVCTKTMVPSMERRDGLSGLINMGNTCFM
SSILQCLIHNPYFIRHSMSQIHSNNCKVRSPDKCFSCALDKIVHELYGAL
STNRQTGFIYLLTCAWKINQQQDAHEFWQFIINQIHQSYVLDLPNAKEVS
RANNKQCECIVHTVFEGSLESSIVCPGCQNNSKTTIDPFLDLSLDIKDKK
KLYECLDSFHKKEQCGECNSAIKQLGIHKLPSVLVLQLKRFEHLLNGSNR
KLDDFIEFPTYLNMKNYCSTKVPDIIYELIGIVSHKGTVNEGHYIAFCKI
SGGQWFKFNDSMVSSISQEEVLKEQAYLLFYTIRQVN
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 chain4fk5 Chain A Residue 504 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4fk5 A Role for Intersubunit Interactions in Maintaining SAGA Deubiquitinating Module Structure and Activity.
Resolution2.032 Å
Binding residue
(original residue number in PDB)
H170 C174 C182 C185
Binding residue
(residue number reindexed from 1)
H172 C176 C184 C187
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) N141 C146 H427 N443
Catalytic site (residue number reindexed from 1) N143 C148 H393 N409
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:4fk5, PDBe:4fk5, PDBj:4fk5
PDBsum4fk5
PubMed22771212
UniProtP50102|UBP8_YEAST Ubiquitin carboxyl-terminal hydrolase 8 (Gene Name=UBP8)

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