Structure of PDB 6fvw Chain J Binding Site BS02

Receptor Information
>6fvw Chain J (length=403) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AAVTSSNIVLETHESGIKPYFEQKIQETELKIRSKTENVRRLEAQRNALN
DKVRFIKDELRLLQEPGSYVGEVIKIVSDKKVLVKVQPEGKYIVDVAKDI
NVKDLKASQRVCLRSDSYMLHKVLENKADPLVSLMMVEKVPDSTYDMVGG
LTKQIKEIKEVIELPVKHPELFESLGIAQPKGVILYGPPGTGKTLLARAV
AHHTDCKFIRVSGAELVQKYIGEGSRMVRELFVMAREHAPSIIFMDEIDS
IGSTRVEGSGGGDSEVQRTMLELLNQLDGFETSKNIKIIMATNRLDILDP
ALLRPGRIDRKIEFPPPSVAARAEILRIHSRKMNLTRGINLRKVAEKMNG
CSGADVKGVCTEAGMYALRERRIHVTQEDFELAVGKVMNKNQETAISVAK
LFK
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 chain6fvw Chain J Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6fvw Expanded Coverage of the 26S Proteasome Conformational Landscape Reveals Mechanisms of Peptidase Gating.
Resolution4.5 Å
Binding residue
(original residue number in PDB)		M149 G192 T193 K195 T196 L197 I327 H331 G355 A356 K359
Binding residue
(residue number reindexed from 1)		M147 G190 T191 K193 T194 L195 I325 H329 G353 A354 K357
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:6fvw, PDBe:6fvw, PDBj:6fvw
PDBsum6fvw
PubMed30067984
UniProtQ01939|PRS8_YEAST 26S proteasome regulatory subunit 8 homolog (Gene Name=RPT6)

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