Structure of PDB 5j2t Chain A

Receptor sequence
>5j2tA (length=439) Species: 9913 (Bos taurus) [Search protein sequence]
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFN
TFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAA
NNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFT
SLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC
AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNV
DLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTG
FKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDS
3D structure
PDB5j2t Structural Basis of Microtubule Destabilization by Potent Auristatin Anti-Mitotics.
ChainA
Resolution2.2 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 G10 Q11 A12 Q15 D98 A99 N101 S140 G143 G144 T145 G146 V177 E183 N206 Y224 N228 G10 Q11 A12 Q15 D98 A99 N101 S140 G143 G144 T145 G146 V177 E183 N206 Y224 N228
BS02 MG A D69 E71 D69 E71
BS03 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:0005829 cytosol
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:5j2t, PDBe:5j2t, PDBj:5j2t
PDBsum5j2t
PubMed27518442
UniProtP81947|TBA1B_BOVIN Tubulin alpha-1B chain

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