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5W3F

Yeast tubulin polymerized with GTP in vitro

Functional Information from GO Data
ChainGOidnamespacecontents
A0000070biological_processmitotic sister chromatid segregation
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0000280biological_processnuclear division
A0003674molecular_functionmolecular_function
A0005200molecular_functionstructural constituent of cytoskeleton
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005819cellular_componentspindle
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0006996biological_processorganelle organization
A0007017biological_processmicrotubule-based process
A0016787molecular_functionhydrolase activity
A0030473biological_processnuclear migration along microtubule
A0034399cellular_componentnuclear periphery
A0045143biological_processhomologous chromosome segregation
A0045298cellular_componenttubulin complex
A0046872molecular_functionmetal ion binding
A0098863biological_processnuclear migration by microtubule mediated pushing forces
B0000022biological_processmitotic spindle elongation
B0000226biological_processmicrotubule cytoskeleton organization
B0000278biological_processmitotic cell cycle
B0003924molecular_functionGTPase activity
B0005200molecular_functionstructural constituent of cytoskeleton
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0006996biological_processorganelle organization
B0007010biological_processcytoskeleton organization
B0007017biological_processmicrotubule-based process
B0031122biological_processcytoplasmic microtubule organization
B0045298cellular_componenttubulin complex
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
B0090307biological_processmitotic spindle assembly
B0090316biological_processpositive regulation of intracellular protein transport
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue MG A 501
ChainResidue
AGLN11
AGLU72
AGTP502

site_idAC2
Number of Residues18
Detailsbinding site for residue GTP A 502
ChainResidue
ASER141
AGLY144
AGLY145
ATHR146
AGLY147
AGLU184
AASN207
APHE225
ALEU228
AASN229
AILE232
AMG501
AGLY10
AGLN11
AALA12
AGLN15
AALA101
AASN103

site_idAC3
Number of Residues12
Detailsbinding site for residue GDP B 600
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BSER138
BGLY141
BGLY142
BTHR143
BGLY144
BASP177
BASN204
BASN226

Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
BGLY140-GLY146
AGLY143-GLY149

site_idPS00228
Number of Residues4
DetailsTUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI
ChainResidueDetails
BMET1-ILE4

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q13509
ChainResidueDetails
BGLN11
BSER138
BGLY142
BTHR143
BGLY144
BASN204
BASN226

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
BGLU69
AGLU72
ASER141
AGLY145
ATHR146
ATHR180
AASN207
AASN229

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
BSER278
BSER280

220113

PDB entries from 2024-05-22

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