Structure of PDB 8shg Chain Z Binding Site BS02

Receptor Information
>8shg 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 IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain8shg Chain Z Residue 602 [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]
PDB8shg Visualizing the chaperone-mediated folding trajectory of the G protein beta5 beta-propeller structure
Resolution2.8 Å
Binding residue
(original residue number in PDB)		D90 K159
Binding residue
(residue number reindexed from 1)		D89 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:8shg, PDBe:8shg, PDBj:8shg
PDBsum8shg
PubMed37852256
UniProtP40227|TCPZ_HUMAN T-complex protein 1 subunit zeta (Gene Name=CCT6A)

[Back to BioLiP]