Structure of PDB 4fip Chain E Binding Site BS05

Receptor Information
>4fip Chain E (length=441) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MSICPHIQQVFQNEKSKDGVLKTCNAARYILNHSVPKEKFLNTMKCGTCH
EINSGATFMCLQCGFCGCWNHSHFLSHSKQIGHIFGINSNNGLLFCFKCE
DYIGNIDLINDAILAKYWDDVCTKTMVPSMERRDGLSGLINMGNTCFMSS
ILQCLIHNPYFIRHSMSQIHSNNCKVRSPDKCFSCALDKIVHELYGALNR
QTGFIYLLTCAWKINQNLAGYSQQDAHEFWQFIINQIHQSYVLDLPNNKQ
CECIVHTVFEGSLESSIVCPGCQNNSKTTIDPFLDLSLDIKDKKKLYECL
DSFHKKEQLKDFNYHCGECNSTQDAIKQLGIHKLPSVLVLQLKRFEHLLN
GSNRKLDDFIEFPTYLNMKNYCSTKVPDIIYELIGIVSHKGTVNEGHYIA
FCKISGGQWFKFNDSMVSSISQEEVLKEQAYLLFYTIRQVN
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 chain4fip Chain E Residue 505 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4fip A Role for Intersubunit Interactions in Maintaining SAGA Deubiquitinating Module Structure and Activity.
Resolution2.686 Å
Binding residue
(original residue number in PDB)
C60 C63 H77 H83
Binding residue
(residue number reindexed from 1)
C60 C63 H77 H83
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) N141 C146 H427 N443
Catalytic site (residue number reindexed from 1) N141 C146 H397 N413
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:4fip, PDBe:4fip, PDBj:4fip
PDBsum4fip
PubMed22771212
UniProtP50102|UBP8_YEAST Ubiquitin carboxyl-terminal hydrolase 8 (Gene Name=UBP8)

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