Structure of PDB 5ylj Chain B

Receptor sequence
>5yljB (length=428) Species: 9823 (Sus scrofa) [Search protein sequence]
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVY
YNEATGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNN
WAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTL
LISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETY
CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADL
RKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMM
AACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVK
TAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDA
3D structure
PDB5ylj The compound millepachine and its derivatives inhibit tubulin polymerization by irreversibly binding to the colchicine-binding site in beta-tubulin.
ChainB
Resolution2.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GDP B G10 Q11 C12 S138 G141 G142 T143 D177 E181 N204 Y222 N226 G10 Q11 C12 S138 G141 G142 T143 D177 E181 N204 Y222 N226
BS02 8X0 B V236 C239 L246 A248 L253 N256 N348 K350 A352 V236 C239 L246 A248 L253 N256 N348 K350 A352 PDBbind-CN: -logKd/Ki=3.86,Kd=139.3uM
Gene Ontology
Molecular Function
GO:0003924 GTPase activity
GO:0005200 structural constituent of cytoskeleton
GO:0005515 protein binding
GO:0005525 GTP binding
GO:0046872 metal ion binding
Biological Process
GO:0000226 microtubule cytoskeleton organization
GO:0000278 mitotic cell cycle
GO:0007017 microtubule-based process
Cellular Component
GO:0005737 cytoplasm
GO:0005856 cytoskeleton
GO:0005874 microtubule

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5ylj, PDBe:5ylj, PDBj:5ylj
PDBsum5ylj
PubMed29691282
UniProtP02554|TBB_PIG Tubulin beta chain

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