Structure of PDB 6fvx Chain H Binding Site BS01

Receptor Information
>6fvx Chain H (length=426) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AAPYAAKLKQTENDLKDIEARIKEKAGVKESDTGLAPSHLWDIMGDRQRL
GEEHPLQVARCTKIIKGNGESDETTTDNNNSGNSNSNSNQQSTDADEDDE
DAKYVINLKQIAKFVVGLGERVSPTDIEEGMRVGVDRSKYNIELPLPPRI
DPSVTMMTVEEKPDVTYSDVGGCKDQIEKLREVVELPLLSPERFATLGID
PPKGILLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMV
RELFEMARTKKACIIFFDEIDAVGGARFDDGAGGDNEVQRTMLELITQLD
GFDPRGNIKVMFATNRPNTLDPALLRPGRIDRKVEFSLPDLEGRANIFRI
HSKSMSVERGIRWELISRLCPNSTGAELRSVCTEAGMFAIRARRKVATEK
DFLKAVDKVISGYKKFSSTSRYMQYN
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 chain6fvx Chain H 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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PDB6fvx Expanded Coverage of the 26S Proteasome Conformational Landscape Reveals Mechanisms of Peptidase Gating.
Resolution4.9 Å
Binding residue
(original residue number in PDB)		G212 P252 G253 T254 G255 K256 T257 L258 R261 E310 I388 G416 A417
Binding residue
(residue number reindexed from 1)		G171 P211 G212 T213 G214 K215 T216 L217 R220 E269 I347 G375 A376
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:0031625 ubiquitin protein ligase binding
GO:0036402 proteasome-activating activity
Biological Process
GO:0006511 ubiquitin-dependent protein catabolic process
GO:0010604 positive regulation of macromolecule metabolic process
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
GO:0045732 positive regulation of protein catabolic process
GO:0045899 positive regulation of RNA polymerase II transcription preinitiation complex assembly
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6fvx, PDBe:6fvx, PDBj:6fvx
PDBsum6fvx
PubMed30067984
UniProtP33299|PRS7_YEAST 26S proteasome regulatory subunit 7 homolog (Gene Name=RPT1)

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