Structure of PDB 7nvm Chain Z Binding Site BS01
Receptor Information
>7nvm Chain Z (length=525) Species:
9606
(Homo sapiens) [
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AAVKTLNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGA
GDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGE
LLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREMDRETLIDV
ARTSLRTKVHAELADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSE
TDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYK
SAEEREKLVKAERKFIEDRVKKIIELKRKVCGDSDKGFVVINQKGIDPFS
LDALSKEGIVALRRAKRRNMERLTLACGGVALNSFDDLSPDCLGHAGLVY
EYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNA
IDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVL
AQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVWDNYCVK
KQLLHSCTVIATNILLVDEIMRAGM
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
7nvm Chain Z Residue 601 [
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Receptor-Ligand Complex Structure
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PDB
7nvm
Snapshots of actin and tubulin folding inside the TRiC chaperonin.
Resolution
3.1 Å
Binding residue
(original residue number in PDB)
L38 D90 G91 T93 S94 T158 K159 A411 L481 D496
Binding residue
(residue number reindexed from 1)
L37 D89 G90 T92 S93 T157 K158 A410 L480 D495
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: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
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Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:7nvm
,
PDBe:7nvm
,
PDBj:7nvm
PDBsum
7nvm
PubMed
35449234
UniProt
P40227
|TCPZ_HUMAN T-complex protein 1 subunit zeta (Gene Name=CCT6A)
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