Structure of PDB 5vfp Chain E Binding Site BS02

Receptor Information
>5vfp Chain E (length=375) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KLLEHKEIDGRLKELREQLKELTKQYEKSENDLKALQSVGQIVGEVLKQL
TEEKFIVKATNGPRYVVGCRRQLDKSKLKPGTRVALDMTTLTIMRYLPRE
VDPLVYNMSHEDPGNVSYSEIGGLSEQIRELREVIELPLTNPELFQRVGI
IPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARL
IREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQM
DGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKIHIDLPNEQARLDILK
IHAGPITKHGEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQ
EDFMKAVRKVADSKKLESKLDYKPV
Ligand information
Ligand IDAGS
InChIInChI=1S/C10H16N5O12P3S/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(25-10)1-24-28(18,19)26-29(20,21)27-30(22,23)31/h2-4,6-7,10,16-17H,1H2,(H,18,19)(H,20,21)(H2,11,12,13)(H2,22,23,31)/t4-,6-,7-,10-/m1/s1
InChIKeyNLTUCYMLOPLUHL-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=S)(O)O)O)O)N
CACTVS 3.370Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=S)[C@@H](O)[C@H]3O
CACTVS 3.370Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=S)[CH](O)[CH]3O
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O)OP(=O)(O)OP(=S)(O)O)O)O)N
ACDLabs 12.01O=P(O)(OP(=S)(O)O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
FormulaC10 H16 N5 O12 P3 S
NamePHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER;
ATP-GAMMA-S;
ADENOSINE 5'-(3-THIOTRIPHOSPHATE);
ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE);
ADENOSINE-5'-DIPHOSPHATE MONOTHIOPHOSPHATE
ChEMBLCHEMBL131890
DrugBankDB02930
ZINCZINC000008295128
PDB chain5vfp Chain E Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5vfp Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome.
Resolution4.2 Å
Binding residue
(original residue number in PDB)		P176 G177 G179 K180 T181 N280 I312 G340 A341 R344
Binding residue
(residue number reindexed from 1)		P162 G163 G165 K166 T167 N266 I298 G326 A327 R330
Annotation score4
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0030674 protein-macromolecule adaptor activity
GO:0036402 proteasome-activating activity
GO:0042802 identical protein binding
Biological Process
GO:0036503 ERAD pathway
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
GO:0045899 positive regulation of RNA polymerase II transcription preinitiation complex assembly
GO:0090261 positive regulation of inclusion body assembly
GO:1901800 positive regulation of proteasomal protein catabolic process
Cellular Component
GO:0000502 proteasome complex
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0008540 proteasome regulatory particle, base subcomplex
GO:0016020 membrane
GO:0016234 inclusion body
GO:0022624 proteasome accessory complex
GO:0031597 cytosolic proteasome complex
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5vfp, PDBe:5vfp, PDBj:5vfp
PDBsum5vfp
PubMed29636472
UniProtP62333|PRS10_HUMAN 26S proteasome regulatory subunit 10B (Gene Name=PSMC6)

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