Structure of PDB 6vpp Chain A Binding Site BS02
Receptor Information
>6vpp Chain A (length=428) Species:
9823
(Sus scrofa) [
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RECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSFNTFFSETGAGKH
VPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIG
KEIIDLVLDRIRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDY
GKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYD
ICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVP
YPRAHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGK
YMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYEPPT
VVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGE
GMEEGEFSEAREDMAALEKDYEEVGVDS
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
6vpp Chain A Residue 502 [
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Receptor-Ligand Complex Structure
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PDB
6vpp
The kinesin-5 tail domain directly modulates the mechanochemical cycle of the motor domain for anti-parallel microtubule sliding.
Resolution
4.4 Å
Binding residue
(original residue number in PDB)
Q11 E71
Binding residue
(residue number reindexed from 1)
Q10 E60
Annotation score
1
Enzymatic activity
Enzyme Commision number
3.6.5.-
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
GO:0031514
motile cilium
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:6vpp
,
PDBe:6vpp
,
PDBj:6vpp
PDBsum
6vpp
PubMed
31958056
UniProt
P02550
|TBA1A_PIG Tubulin alpha-1A chain (Gene Name=TUBA1A)
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