Structure of PDB 8she Chain h Binding Site BS02

Receptor Information
>8she Chain h (length=525) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MMPTPVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIV
DGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLL
AAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVE
QRKLLEKCAMTALSSKLISQQKAFFAKMVVDAVMMLDDLLQLKMIGIKKV
QGGALEDSQLVAGVAFKKTFSYAGFEMQPKKYHNPKIALLNVELELKAEK
DNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVAT
QYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALSADVLGRCQVFEE
TQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAI
KNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLC
DNAGFDATNILNKLRARHAQGGTWYGVDINNEDIADNFEAFVWEPAMVRI
NALTAASEAACLIVSVDETIKNPRS
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 chain8she Chain h 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]
PDB8she Visualizing the chaperone-mediated folding trajectory of the G protein beta 5 beta-propeller structure
Resolution2.8 Å
Binding residue
(original residue number in PDB)
D61 D92 T94 T95
Binding residue
(residue number reindexed from 1)
D61 D92 T94 T95
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:0042802 identical protein 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: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:0005737 cytoplasm
GO:0005829 cytosol
GO:0005832 chaperonin-containing T-complex
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:8she, PDBe:8she, PDBj:8she
PDBsum8she
PubMed37852256
UniProtQ99832|TCPH_HUMAN T-complex protein 1 subunit eta (Gene Name=CCT7)

[Back to BioLiP]