Structure of PDB 8sho Chain g Binding Site BS01
Receptor Information
>8sho Chain g (length=526) Species:
9606
(Homo sapiens) [
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RPVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPM
GGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGE
MLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISDSDMMLN
IINSSITTKAISRWSSLACNIALDAVKMVQFEENGRKEIDIKKYARVEKI
PGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQT
DIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYL
MRANITAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTGAGLLEIKK
IGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLD
PQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQN
CGASTIRLLTSLRAKHTQENCETWGVNGETGTLVDMKELGIWEPLAVKLQ
TYKTAVETAVLLLRIDDIVSGHKKKG
Ligand information
Ligand ID
ADP
InChI
InChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKey
XTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341
Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04
O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341
Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0
c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
Formula
C10 H15 N5 O10 P2
Name
ADENOSINE-5'-DIPHOSPHATE
ChEMBL
CHEMBL14830
DrugBank
DB16833
ZINC
ZINC000012360703
PDB chain
8sho Chain g Residue 601 [
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Receptor-Ligand Complex Structure
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PDB
8sho
Visualizing the chaperone-mediated folding trajectory of the G protein beta 5 beta-propeller structure
Resolution
3.0 Å
Binding residue
(original residue number in PDB)
G42 P43 D93 G94 T95 T96 T162 G410 G411 G482 I495 E497
Binding residue
(residue number reindexed from 1)
G38 P39 D89 G90 T91 T92 T158 G406 G407 G478 I491 E493
Annotation score
5
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: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:0002199
zona pellucida receptor complex
GO:0005737
cytoplasm
GO:0005829
cytosol
GO:0005832
chaperonin-containing T-complex
GO:0005856
cytoskeleton
GO:0005874
microtubule
GO:0044297
cell body
GO:0070062
extracellular exosome
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:8sho
,
PDBe:8sho
,
PDBj:8sho
PDBsum
8sho
PubMed
37852256
UniProt
P49368
|TCPG_HUMAN T-complex protein 1 subunit gamma (Gene Name=CCT3)
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