9G0Q

Xenopus laevis undecorated microtubule - 15 protofilament, 3-start helix

External Resource: Annotation

Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	Tubulin beta-4 chain	structural constituent of cytoskeleton structural molecule activity binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding organic cyclic compound binding purine nucleotide binding anion binding structural constituent of cytoskeleton structural molecule activity binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding organic cyclic compound binding purine nucleotide binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding cation binding metal ion binding pyrophosphatase activity GTPase activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity	cellular process cell cycle mitotic cell cycle cellular component organization organelle organization microtubule cytoskeleton organization microtubule-based process cellular component organization or biogenesis cytoskeleton organization	cellular anatomical structure intracellular anatomical structure cytoplasm polymeric cytoskeletal fiber intracellular membraneless organelle intracellular organelle cytoskeleton organelle membraneless organelle supramolecular fiber microtubule supramolecular polymer supramolecular complex microtubule cytoskeleton
G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], L [auth f]	Tubulin alpha chain	structural constituent of cytoskeleton structural molecule activity hydrolase activity catalytic activity binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding organic cyclic compound binding structural constituent of cytoskeleton structural molecule activity hydrolase activity catalytic activity binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding organic cyclic compound binding purine nucleotide binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding	cellular process cell cycle mitotic cell cycle cellular component organization organelle organization microtubule cytoskeleton organization microtubule-based process cellular component organization or biogenesis cytoskeleton organization	cellular anatomical structure intracellular anatomical structure cytoplasm polymeric cytoskeletal fiber intracellular membraneless organelle intracellular organelle cytoskeleton organelle membraneless organelle supramolecular fiber microtubule supramolecular polymer supramolecular complex microtubule cytoskeleton

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR003008	Tubulin/FtsZ, GTPase domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR008280	Tubulin/FtsZ, C-terminal	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR037103	Tubulin/FtsZ-like, C-terminal domain	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR017975	Tubulin, conserved site	Conserved Site
A, B, C, D, E A, B, C, D, E, F	IPR000217	Tubulin	Family
A, B, C, D, E A, B, C, D, E, F	IPR023123	Tubulin, C-terminal	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR002453	Beta tubulin	Family
A, B, C, D, E A, B, C, D, E, F	IPR013838	Beta tubulin, autoregulation binding site	Binding Site
A, B, C, D, E A, B, C, D, E, F	IPR018316	Tubulin/FtsZ, 2-layer sandwich domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR036525	Tubulin/FtsZ, GTPase domain superfamily	Homologous Superfamily
G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], L [auth f]	IPR003008	Tubulin/FtsZ, GTPase domain	Domain
G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], L [auth f]	IPR008280	Tubulin/FtsZ, C-terminal	Homologous Superfamily
G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], L [auth f]	IPR037103	Tubulin/FtsZ-like, C-terminal domain	Homologous Superfamily
G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], L [auth f]	IPR017975	Tubulin, conserved site	Conserved Site
G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], L [auth f]	IPR002452	Alpha tubulin	Family
G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], L [auth f]	IPR000217	Tubulin	Family
G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], L [auth f]	IPR023123	Tubulin, C-terminal	Homologous Superfamily
G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], L [auth f]	IPR018316	Tubulin/FtsZ, 2-layer sandwich domain	Domain
G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], G [auth a], H [auth b], I [auth c], J [auth d], K [auth e], L [auth f]	IPR036525	Tubulin/FtsZ, GTPase domain superfamily	Homologous Superfamily

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.