Structure of PDB 5uyz Chain B Binding Site BS01
Receptor Information
>5uyz Chain B (length=488) Species:
9606
(Homo sapiens) [
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LEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSM
MDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHP
IRIADGYEQAARVAIERLDKISDSVLVDIKDTEPLIQTAKSCHRQMAEIA
VNAVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQM
PKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMI
QQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGG
RIVPRFSELTAEKLGFAGLVQETKDKMLVIEQCAVTIFIRGGNKMIIEEA
KRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAM
RAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGT
NDMKQQHVIETLIGKKQQISLATQMVRMILKIDDIRKP
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
5uyz Chain B Residue 601 [
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Receptor-Ligand Complex Structure
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PDB
5uyz
Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.
Resolution
3.6 Å
Binding residue
(original residue number in PDB)
L52 G53 P54 G105 T106 T107 G422 C493 L494 V506 E508
Binding residue
(residue number reindexed from 1)
L22 G23 P24 G75 T76 T77 G374 C445 L446 V458 E460
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 D356
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
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Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:5uyz
,
PDBe:5uyz
,
PDBj:5uyz
PDBsum
5uyz
PubMed
28623285
UniProt
P48643
|TCPE_HUMAN T-complex protein 1 subunit epsilon (Gene Name=CCT5)
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