Structure of PDB 8shp Chain Q Binding Site BS02

Receptor Information
>8shp Chain Q (length=538) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ALHVPKAPGFAQMLKEGAKHFSGLEEAVYRNIQACKELAQTTRTAYGPNG
MNKMVINHLEKLFVTNDAATILRELEVQHPAAKMIVMASHMQEQEVGDGT
NFVLVFAGALLELAEELLRIGLSVSEVIEGYEIACRKAHEILPNLVCCSA
KNLRDIDEVSSLLRTSIMSKQYGNEVFLAKLIAQACVSIFPDSGHFNVDN
IRVCKILGSGISSSSVLHGMVFKKETEGDVTSVKDAKIAVYSCPFDGMIT
ETKGTVLIKTAEELMNFSKGEENLMDAQVKAIADTGANVVVTGGKVADMA
LHYANKYNIMLVRLNSKWDLRRLCKTVGATALPRLTPPVLEEMGHCDSVY
LSEVGDTQVVVFKHEKEDGAISTIVLRGSTDNLMDDIERAVDDGVNTFKV
LTRDKRLVPGGGATEIELAKQITSYGETCPGLEQYAIKKFAEAFEAIPRA
LAENSGVKANEVISKLYAVHQEGNKNVGLDIEAEVPAVKDMLEAGILDTY
LGKYWAIKLATNAAVTVLRVDQIIMAKPAGGPKPPSGK
Ligand information
Ligand IDAF3
InChIInChI=1S/Al.3FH/h;3*1H/q+3;;;/p-3
InChIKeyKLZUFWVZNOTSEM-UHFFFAOYSA-K
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		F[Al](F)F
FormulaAl F3
NameALUMINUM FLUORIDE
ChEMBL
DrugBank
ZINC
PDB chain8shp Chain Q Residue 603 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB8shp Visualizing the chaperone-mediated folding trajectory of the G protein beta 5 beta-propeller structure
Resolution3.0 Å
Binding residue
(original residue number in PDB)		D68 D99 G100 T101 K171
Binding residue
(residue number reindexed from 1)		D67 D98 G99 T100 K170
Annotation score1
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0044183 protein folding chaperone
GO:0045296 cadherin binding
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
GO:0007339 binding of sperm to zona pellucida
GO:0032212 positive regulation of telomere maintenance via telomerase
GO:0050821 protein stabilization
GO:0051086 chaperone mediated protein folding independent of cofactor
GO:0061077 chaperone-mediated protein folding
GO:1904871 positive regulation of protein localization to Cajal body
GO:1904874 positive regulation of telomerase RNA localization to Cajal body
Cellular Component
GO:0002199 zona pellucida receptor complex
GO:0005576 extracellular region
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005813 centrosome
GO:0005829 cytosol
GO:0005832 chaperonin-containing T-complex
GO:0005856 cytoskeleton
GO:0005874 microtubule
GO:0005929 cilium
GO:0034774 secretory granule lumen
GO:0035578 azurophil granule lumen
GO:0044297 cell body
GO:0045111 intermediate filament cytoskeleton
GO:0070062 extracellular exosome
GO:1904813 ficolin-1-rich granule lumen

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:8shp, PDBe:8shp, PDBj:8shp
PDBsum8shp
PubMed37852256
UniProtP50990|TCPQ_HUMAN T-complex protein 1 subunit theta (Gene Name=CCT8)

[Back to BioLiP]