Structure of PDB 8i1u Chain M Binding Site BS02

Receptor Information
>8i1u Chain M (length=525) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YGRPFLIIKDQDRKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMM
VDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVV
LAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKD
TEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVADMERRDVDFELIKV
EGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPK
TKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEAN
HLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVQE
ISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRN
LIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMA
LSENSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQHVIETLI
GKKQQISLATQMVRMILKIDDIRKP
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 chain8i1u Chain M 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]
PDB8i1u Human TRiC-PhLP2A complex in the closed state
Resolution3.24 Å
Binding residue
(original residue number in PDB)		D73 T106 K176 D404
Binding residue
(residue number reindexed from 1)		D62 T95 K165 D393
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:8i1u, PDBe:8i1u, PDBj:8i1u
PDBsum8i1u
PubMed38307855
UniProtP48643|TCPE_HUMAN T-complex protein 1 subunit epsilon (Gene Name=CCT5)

[Back to BioLiP]