Structure of PDB 8shf Chain e Binding Site BS02

Receptor Information
>8shf Chain e (length=540) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ASMGTLAFDEYGRPFLIIKDQDRKSRLMGLEALKSHIMAAKAVANTMRTS
LGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDE
IGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKI
SDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVADMER
RDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAIL
TCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAI
CQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAE
KLGFAGLVQEISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRS
LHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAF
ADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDM
KQQHVIETLIGKKQQISLATQMVRMILKIDDIRKPGESEE
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 chain8shf Chain e 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]
PDB8shf Visualizing the chaperone-mediated folding trajectory of the G protein beta 5 beta-propeller.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		D73 D104 T106 T107 K176 D404
Binding residue
(residue number reindexed from 1)		D72 D103 T105 T106 K175 D403
Annotation score1
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0003730 mRNA 3'-UTR binding
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0031681 G-protein beta-subunit binding
GO:0044183 protein folding chaperone
GO:0048027 mRNA 5'-UTR binding
GO:0048487 beta-tubulin 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:0009615 response to virus
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:0005737 cytoplasm
GO:0005813 centrosome
GO:0005829 cytosol
GO:0005832 chaperonin-containing T-complex
GO:0005856 cytoskeleton
GO:0005874 microtubule
GO:0044297 cell body
GO:0070062 extracellular exosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:8shf, PDBe:8shf, PDBj:8shf
PDBsum8shf
PubMed37852256
UniProtP48643|TCPE_HUMAN T-complex protein 1 subunit epsilon (Gene Name=CCT5)

[Back to BioLiP]