Structure of PDB 3mhs Chain A Binding Site BS04

Receptor Information
>3mhs Chain A (length=455) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AMSICPHIQQVFQNEKSKDGVLKTCNAARYILNHSVPKEKFLNTMKCGTC
HEINSGATFMCLQCGFCGCWNHSHFLSHSKQIGHIFGINSNNGLLFCFKC
EDYIGNIDLINDAILAKYWDDVCTKTMVPSMERRDGLSGLINMGSTCFMS
SILQCLIHNPYFIRHSMSQIHSNNCKVRSPDKCFSCALDKIVHELYGALN
TSTNRQTGFIYLLTCAWKINQNLAGYSQQDAHEFWQFIINQIHQSYVLDL
PNNNKQCECIVHTVFEGSLESSIVCPGCQNNSKTTIDPFLDLSLDIKDKK
KLYECLDSFHKKEQLKDFNYHCGECNSTQDAIKQLGIHKLPSVLVLQLKR
FEHLLNGSNRKLDDFIEFPTYLNMKNYCSTKEKDKENGKVPDIIYELIGI
VSHKGTVNEGHYIAFCKISGGQWFKFNDSMVSSISQEEVLKEQAYLLFYT
IRQVN
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 chain3mhs Chain A Residue 475 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3mhs Structural insights into the assembly and function of the SAGA deubiquitinating module.
Resolution1.89 Å
Binding residue
(original residue number in PDB)		H170 C174 C182 C185
Binding residue
(residue number reindexed from 1)		H171 C175 C183 C186
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) N141 C146 H427 N443
Catalytic site (residue number reindexed from 1) N142 C147 H411 N427
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:3mhs, PDBe:3mhs, PDBj:3mhs
PDBsum3mhs
PubMed20395473
UniProtP50102|UBP8_YEAST Ubiquitin carboxyl-terminal hydrolase 8 (Gene Name=UBP8)

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