Structure of PDB 5uyx Chain D Binding Site BS01
Receptor Information
>5uyx Chain D (length=451) Species:
9606
(Homo sapiens) [
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LEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSM
MDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHP
IRIADGYEQAARVAIEHLDKISDSVLVDIKDTEPLIQTAHRQMAEIAVNA
VLTVADMERRDVDFELIKVTKLIKGVIVDKDFSHPQMPKKVEDAKIAILT
CPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAIC
QWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEK
LGFAGLVQEISDKMLVIEQAVTIFIHDALCVIRNLIRDNRVVYGGGAAEI
SCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEV
RARQVKEMNPALGIDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMI
L
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
5uyx Chain D Residue 601 [
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Receptor-Ligand Complex Structure
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PDB
5uyx
Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.
Resolution
3.5 Å
Binding residue
(original residue number in PDB)
L52 G53 G105 G422 C493 V506
Binding residue
(residue number reindexed from 1)
L22 G23 G75 G345 C416 V429
Annotation score
5
Enzymatic activity
Catalytic site (original residue number in PDB)
D73 T106 T107 D404
Catalytic site (residue number reindexed from 1)
D43 T76 T77 D327
Enzyme Commision number
?
Gene Ontology
Molecular Function
GO:0003730
mRNA 3'-UTR binding
GO:0005515
protein binding
GO:0005524
ATP binding
GO:0016887
ATP hydrolysis activity
GO:0031681
G-protein beta-subunit binding
GO:0044183
protein folding chaperone
GO:0048027
mRNA 5'-UTR binding
GO:0048487
beta-tubulin binding
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:0009615
response to virus
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:0005813
centrosome
GO:0005829
cytosol
GO:0005832
chaperonin-containing T-complex
GO:0005856
cytoskeleton
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:5uyx
,
PDBe:5uyx
,
PDBj:5uyx
PDBsum
5uyx
PubMed
28623285
UniProt
P48643
|TCPE_HUMAN T-complex protein 1 subunit epsilon (Gene Name=CCT5)
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