Structure of PDB 8sgc Chain b Binding Site BS01
Receptor Information
>8sgc Chain b (length=525) Species:
9606
(Homo sapiens) [
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ASLSLAPVNIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKI
LLSSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTS
VTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSD
EVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHI
IKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKI
FGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPE
QLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEE
VMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTV
KDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIA
DNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKR
QVLLSAAEAAEVILRVDNIIKAAPR
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
8sgc Chain b Residue 601 [
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Receptor-Ligand Complex Structure
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PDB
8sgc
Visualizing the chaperone-mediated folding trajectory of the G protein beta 5 beta-propeller structure
Resolution
2.9 Å
Binding residue
(original residue number in PDB)
L43 G44 P45 D97 G98 T100 S101 T165 S168 S169 G410 I450 E495
Binding residue
(residue number reindexed from 1)
L42 G43 P44 D96 G97 T99 S100 T164 S167 S168 G409 I449 E494
Annotation score
5
Enzymatic activity
Enzyme Commision number
?
Gene Ontology
Molecular Function
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: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:0051131
chaperone-mediated protein complex assembly
GO:0061077
chaperone-mediated protein folding
GO:0090666
scaRNA localization to Cajal body
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:0005576
extracellular region
GO:0005737
cytoplasm
GO:0005829
cytosol
GO:0005832
chaperonin-containing T-complex
GO:0005874
microtubule
GO:0035578
azurophil granule lumen
GO:0044297
cell body
GO:0070062
extracellular exosome
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:8sgc
,
PDBe:8sgc
,
PDBj:8sgc
PDBsum
8sgc
PubMed
37852256
UniProt
P78371
|TCPB_HUMAN T-complex protein 1 subunit beta (Gene Name=CCT2)
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