Structure of PDB 7ztd Chain C Binding Site BS01

Receptor Information
>7ztd Chain C (length=366) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGD
EAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLT
EAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSG
DGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAER
EIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFR
CPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMY
PGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMW
ISKQEYDESGPSIVHR
Ligand information
Ligand IDADP
InChIInChI=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
InChIKeyXTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(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 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
FormulaC10 H15 N5 O10 P2
NameADENOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL14830
DrugBankDB16833
ZINCZINC000012360703
PDB chain7ztd Chain C Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB7ztd Structural basis underlying specific biochemical activities of non-muscle tropomyosin isoforms.
Resolution4.6 Å
Binding residue
(original residue number in PDB)
S14 M16 K18 G156 E214 G302 Y306
Binding residue
(residue number reindexed from 1)
S8 M10 K12 G150 E208 G296 Y300
Annotation score5
Enzymatic activity
Enzyme Commision number 3.6.4.-
Gene Ontology
Molecular Function
GO:0005200 structural constituent of cytoskeleton
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016787 hydrolase activity
GO:0016887 ATP hydrolysis activity
GO:0019894 kinesin binding
GO:0019901 protein kinase binding
GO:0030957 Tat protein binding
GO:0031492 nucleosomal DNA binding
GO:0042802 identical protein binding
GO:0048156 tau protein binding
GO:0050998 nitric-oxide synthase binding
GO:0098973 structural constituent of postsynaptic actin cytoskeleton
Biological Process
GO:0000079 regulation of cyclin-dependent protein serine/threonine kinase activity
GO:0001738 morphogenesis of a polarized epithelium
GO:0006338 chromatin remodeling
GO:0006357 regulation of transcription by RNA polymerase II
GO:0007010 cytoskeleton organization
GO:0007163 establishment or maintenance of cell polarity
GO:0007409 axonogenesis
GO:0008284 positive regulation of cell population proliferation
GO:0021762 substantia nigra development
GO:0022898 regulation of transmembrane transporter activity
GO:0030071 regulation of mitotic metaphase/anaphase transition
GO:0032091 negative regulation of protein binding
GO:0034333 adherens junction assembly
GO:0035633 maintenance of blood-brain barrier
GO:0042981 regulation of apoptotic process
GO:0045176 apical protein localization
GO:0045582 positive regulation of T cell differentiation
GO:0045596 negative regulation of cell differentiation
GO:0045597 positive regulation of cell differentiation
GO:0045663 positive regulation of myoblast differentiation
GO:0045893 positive regulation of DNA-templated transcription
GO:0048870 cell motility
GO:0051621 regulation of norepinephrine uptake
GO:0051623 positive regulation of norepinephrine uptake
GO:0051726 regulation of cell cycle
GO:0070316 regulation of G0 to G1 transition
GO:0070527 platelet aggregation
GO:0071896 protein localization to adherens junction
GO:0072749 cellular response to cytochalasin B
GO:0098974 postsynaptic actin cytoskeleton organization
GO:0150111 regulation of transepithelial transport
GO:1900242 regulation of synaptic vesicle endocytosis
GO:1902459 positive regulation of stem cell population maintenance
GO:1903076 regulation of protein localization to plasma membrane
GO:1905168 positive regulation of double-strand break repair via homologous recombination
GO:2000045 regulation of G1/S transition of mitotic cell cycle
GO:2000779 regulation of double-strand break repair
GO:2000781 positive regulation of double-strand break repair
GO:2000819 regulation of nucleotide-excision repair
Cellular Component
GO:0000776 kinetochore
GO:0000785 chromatin
GO:0000786 nucleosome
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005856 cytoskeleton
GO:0005884 actin filament
GO:0005886 plasma membrane
GO:0005903 brush border
GO:0005911 cell-cell junction
GO:0005912 adherens junction
GO:0005925 focal adhesion
GO:0015629 actin cytoskeleton
GO:0016020 membrane
GO:0016363 nuclear matrix
GO:0016514 SWI/SNF complex
GO:0016586 RSC-type complex
GO:0030027 lamellipodium
GO:0030424 axon
GO:0030863 cortical cytoskeleton
GO:0031982 vesicle
GO:0032991 protein-containing complex
GO:0035060 brahma complex
GO:0035267 NuA4 histone acetyltransferase complex
GO:0036464 cytoplasmic ribonucleoprotein granule
GO:0043296 apical junction complex
GO:0044305 calyx of Held
GO:0045202 synapse
GO:0070062 extracellular exosome
GO:0070160 tight junction
GO:0071564 npBAF complex
GO:0071565 nBAF complex
GO:0072562 blood microparticle
GO:0097433 dense body
GO:0098685 Schaffer collateral - CA1 synapse
GO:0098793 presynapse
GO:0098871 postsynaptic actin cytoskeleton
GO:0098978 glutamatergic synapse
GO:0140092 bBAF complex
GO:0140288 GBAF complex
GO:1990904 ribonucleoprotein complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:7ztd, PDBe:7ztd, PDBj:7ztd
PDBsum7ztd
PubMed36586407
UniProtP60709|ACTB_HUMAN Actin, cytoplasmic 1 (Gene Name=ACTB)

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