Structure of PDB 6ef3 Chain J Binding Site BS01

Receptor Information
>6ef3 Chain J (length=383) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
FEQKIQETELKIRSKTENVRRLEAQRNALNDKVRFIKDELRLLQEPGSYV
GEVIKIVSDKKVLVKVQPEGKYIVDVAKDINVKDLKASQRVCLRSDSYML
HKVLENKADPLVSLMMVEKVPDSTYDMVGGLTKQIKEIKEVIELPVKHPE
LFESLGIAQPKGVILYGPPGTGKTLLARAVAHHTDCKFIRVSGAELVQKY
IGEGSRMVRELFVMAREHAPSIIFMDEIDSIGSTRVEGSGGGDSEVQRTM
LELLNQLDGFETSKNIKIIMATNRLDILDPALLRPGRIDRKIEFPPPSVA
ARAEILRIHSRKMNLTRGINLRKVAEKMNGCSGADVKGVCTEAGMYALRE
RRIHVTQEDFELAVGKVMNKNQETAISVAKLFK
Ligand information
Ligand IDATP
InChIInChI=1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyZKHQWZAMYRWXGA-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=O)(O)O[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@](O)(=O)O[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
FormulaC10 H16 N5 O13 P3
NameADENOSINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL14249
DrugBankDB00171
ZINCZINC000004261765
PDB chain6ef3 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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PDB6ef3 Substrate-engaged 26Sproteasome structures reveal mechanisms for ATP-hydrolysis-driven translocation.
Resolution4.17 Å
Binding residue
(original residue number in PDB)		T193 G194 K195 T196 N295 I327 H331 G355 A356
Binding residue
(residue number reindexed from 1)		T171 G172 K173 T174 N273 I305 H309 G333 A334
Annotation score5
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0019904 protein domain specific binding
GO:0031625 ubiquitin protein ligase binding
GO:0036402 proteasome-activating activity
Biological Process
GO:0006289 nucleotide-excision repair
GO:0006338 chromatin remodeling
GO:0010604 positive regulation of macromolecule metabolic process
GO:0032968 positive regulation of transcription elongation by RNA polymerase II
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
GO:0045899 positive regulation of RNA polymerase II transcription preinitiation complex assembly
GO:0070651 nonfunctional rRNA decay
GO:0070682 proteasome regulatory particle assembly
GO:1901800 positive regulation of proteasomal protein catabolic process
Cellular Component
GO:0000502 proteasome complex
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0008540 proteasome regulatory particle, base subcomplex
GO:0034515 proteasome storage granule

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6ef3, PDBe:6ef3, PDBj:6ef3
PDBsum6ef3
PubMed30309908
UniProtQ01939|PRS8_YEAST 26S proteasome regulatory subunit 8 homolog (Gene Name=RPT6)

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