Structure of PDB 6u0t Chain E

Receptor sequence
>6u0tE (length=429) Species: 5911 (Tetrahymena thermophila) [Search protein sequence]
MREVISIHVGQGGIQVGNACWELFCLEHGIQPDGQMPAFNTFFSETGAGK
HVPRAVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTI
GKEIVDLCLDRIRKLADNCTGLQGFLVFNSVGGGTGSGLGSLLLERLSVD
YGKKSKLGFTIYPSPQVSTAVVEPYNSILSTHSLLEHTDVAVMLDNEAIY
DICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDITEFQTNLV
PYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHG
KYMACSMMYRGDVVPKDVNASIATIKTKRTIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVMRAVCMISNSTAIAEVFSRLDHKFDLMYAKRAFVHWYVG
EGMEEGEFSEAREDLAALEKDYEEVGIET
3D structure
PDB6u0t Tubulin lattice in cilia is in a stressed form regulated by microtubule inner proteins.
ChainE
Resolution4.16 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 E G10 Q11 G12 E71 A99 A100 S140 G143 G144 T145 G146 I171 T179 Y224 L227 G10 Q11 G12 E61 A89 A90 S130 G133 G134 T135 G136 I161 T169 Y214 L217
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:6u0t, PDBe:6u0t, PDBj:6u0t
PDBsum6u0t
PubMed31527277
UniProtP41351|TBA_TETTH Tubulin alpha chain

[Back to BioLiP]