Structure of PDB 5ylj Chain A

Receptor sequence
>5yljA (length=437) Species: 9823 (Sus scrofa) [Search protein sequence]
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFN
TFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAA
NNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFT
SLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC
AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNV
DLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTG
FKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGV
3D structure
PDB5ylj The compound millepachine and its derivatives inhibit tubulin polymerization by irreversibly binding to the colchicine-binding site in beta-tubulin.
ChainA
Resolution2.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.5.-
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 GTP A Q11 A12 Q15 A99 N101 S140 G143 G144 T145 G146 V177 T179 E183 N206 Y224 N228 Q11 A12 Q15 A99 N101 S140 G143 G144 T145 G146 V177 T179 E183 N206 Y224 N228
BS02 CA A D39 T41 G44 E55 D39 T41 G44 E55
Gene Ontology
Molecular Function
GO:0003924 GTPase activity
GO:0005200 structural constituent of cytoskeleton
GO:0005525 GTP binding
GO:0016787 hydrolase activity
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
GO:0015630 microtubule cytoskeleton

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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
UniProtQ2XVP4|TBA1B_PIG Tubulin alpha-1B chain (Gene Name=TUBA1B)

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