Structure of PDB 6o2r Chain K

Receptor sequence
>6o2rK (length=432) Species: 9823 (Sus scrofa) [Search protein sequence]
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPDSFNTFFSETGAG
KHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYT
IGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSV
DYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAI
YDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNL
VPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRH
GKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQP
PTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYV
GEGMEEGEFSEAREDMAALEKDYEEVGVDSVE
3D structure
PDB6o2r Effects of alpha-tubulin acetylation on microtubule structure and stability.
ChainK
Resolution3.3 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 K G10 Q11 A12 Q15 A99 A100 N101 G143 G144 T145 T179 N206 Y224 N228 G10 Q11 A12 Q15 A90 A91 N92 G134 G135 T136 T170 N197 Y215 N219
BS02 MG K D69 E71 D60 E62
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6o2r, PDBe:6o2r, PDBj:6o2r
PDBsum6o2r
PubMed31072936
UniProtQ2XVP4|TBA1B_PIG Tubulin alpha-1B chain (Gene Name=TUBA1B)

[Back to BioLiP]