Structure of PDB 8utr Chain A Binding Site BS02
Receptor Information
>8utr Chain A (length=440) Species:
9823
(Sus scrofa) [
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MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFN
TFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAA
NNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFT
SLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC
AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNV
DLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTG
FKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV
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
8utr Chain A Residue 502 [
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Receptor-Ligand Complex Structure
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PDB
8utr
Cryo-EM of human KIF1A reveals its mechanism of motility and the effect of its pathogenic variant P305L
Resolution
3.3 Å
Binding residue
(original residue number in PDB)
E71 D98
Binding residue
(residue number reindexed from 1)
E71 D98
Annotation score
1
Enzymatic activity
Enzyme Commision number
3.6.5.-
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
Cellular Component
GO:0005737
cytoplasm
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:8utr
,
PDBe:8utr
,
PDBj:8utr
PDBsum
8utr
PubMed
38956021
UniProt
Q2XVP4
|TBA1B_PIG Tubulin alpha-1B chain (Gene Name=TUBA1B)
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