Structure of PDB 4yj3 Chain A

Receptor sequence

>4yj3A (length=438) Species: 9913 (Bos taurus)

MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFN
TFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAA
NNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFT
SLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC
AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNV
DLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTG
FKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVD

3D structure

• PDB: 4yj3 Structures of potent anticancer compounds bound to tubulin.
• Chain: A
• Resolution: 3.75 Å

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	G10 Q11 A12 A99 N101 S140 G143 G144 T145 V177 S178 T179 E183 N206 Y224 N228	G10 Q11 A12 A99 N101 S140 G143 G144 T145 V177 S178 T179 E183 N206 Y224 N228
BS02	CA	A	D39 T41 G44 E55	D39 T41 G44 E55
BS03	4EE	A	T179 V181	T179 V181

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:0005829 cytosol
• GO:0005856 cytoskeleton
• GO:0005874 microtubule
• GO:0015630 microtubule cytoskeleton

External links

• PDB: RCSB:4yj3, PDBe:4yj3, PDBj:4yj3
• PDBsum: 4yj3
• PubMed: 25970265
• UniProt: P81947|TBA1B_BOVIN Tubulin alpha-1B chain