Structure of PDB 1sa0 Chain A

Receptor sequence
>1sa0A (length=427) Species: 9913 (Bos taurus) [Search protein sequence]
RECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTI
GKEIIDLVLDRIRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIY
DICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLV
PYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHG
KYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYEPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVG
EGMEEGEFSEAREDMAALEKDYEEVGV
3D structure
PDB1sa0 Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain.
ChainA
Resolution3.58 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 A G10 Q11 A12 Q15 E71 D98 S140 G143 G144 T145 S178 E183 N206 Y224 N228 G9 Q10 A11 Q14 E61 D88 S130 G133 G134 T135 S168 E173 N196 Y214 N218
BS02 CN2 A S178 V181 S168 V171
Gene Ontology
Molecular Function
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1sa0, PDBe:1sa0, PDBj:1sa0
PDBsum1sa0
PubMed15014504
UniProtQ2HJ86|TBA1D_BOVIN Tubulin alpha-1D chain (Gene Name=TUBA1D)

[Back to BioLiP]