Structure of PDB 8sff Chain A Binding Site BS02

Receptor Information
>8sff Chain A (length=536) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EGPLSVFGDRSTGETIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGD
VTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELL
KNADELVKQKIHPTSVISGYRLACKEAVRYINENLIVNTDELGRDCLINA
AKTSMSSKIIGINGDFFANMVVDAVLAIKYTDIRGQPRYPVNSVNILKAH
GRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQ
VVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFV
EAGAMAVRRVLKRDLKRIAKASGATILSTLANLEGEETFEAAMLGQAEEV
VQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKR
VLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNT
LAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLSNGKPRDNKQA
GVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPES
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 chain8sff Chain A 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]
PDB8sff Visualizing the chaperone-mediated folding trajectory of the G protein beta 5 beta-propeller structure
Resolution3.2 Å
Binding residue
(original residue number in PDB)		D57 D88 K159 D394
Binding residue
(residue number reindexed from 1)		D56 D87 K158 D393
Annotation score1
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0031625 ubiquitin protein ligase binding
GO:0044183 protein folding chaperone
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
GO:0007021 tubulin complex assembly
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:0090666 scaRNA localization to Cajal body
GO:1904851 positive regulation of establishment of protein localization to telomere
GO:1904871 positive regulation of protein localization to Cajal body
GO:1904874 positive regulation of telomerase RNA localization to Cajal body
Cellular Component
GO:0000242 pericentriolar material
GO:0000792 heterochromatin
GO:0001669 acrosomal vesicle
GO:0002199 zona pellucida receptor complex
GO:0005737 cytoplasm
GO:0005794 Golgi apparatus
GO:0005813 centrosome
GO:0005815 microtubule organizing center
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:8sff, PDBe:8sff, PDBj:8sff
PDBsum8sff
PubMed37852256
UniProtP17987|TCPA_HUMAN T-complex protein 1 subunit alpha (Gene Name=TCP1)

[Back to BioLiP]