Structure of PDB 7nvl Chain z Binding Site BS02

Receptor Information
>7nvl Chain z (length=525) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AAVKTLNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGA
GDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGE
LLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREMDRETLIDV
ARTSLRTKVHAELADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSE
TDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYK
SAEEREKLVKAERKFIEDRVKKIIELKRKVCGDSDKGFVVINQKGIDPFS
LDALSKEGIVALRRAKRRNMERLTLACGGVALNSFDDLSPDCLGHAGLVY
EYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNA
IDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVL
AQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVWDNYCVK
KQLLHSCTVIATNILLVDEIMRAGM
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 chain7nvl Chain z 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]
PDB7nvl Snapshots of actin and tubulin folding inside the TRiC chaperonin.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		D59 D90 T92 T93 K159
Binding residue
(residue number reindexed from 1)		D58 D89 T91 T92 K158
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:0044183 protein folding chaperone
GO:0051082 unfolded protein binding
GO:0071987 WD40-repeat domain binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
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: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:0005737 cytoplasm
GO:0005829 cytosol
GO:0005832 chaperonin-containing T-complex
GO:0005874 microtubule
GO:0070062 extracellular exosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:7nvl, PDBe:7nvl, PDBj:7nvl
PDBsum7nvl
PubMed35449234
UniProtP40227|TCPZ_HUMAN T-complex protein 1 subunit zeta (Gene Name=CCT6A)

[Back to BioLiP]