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3CB2

Crystal structure of human gamma-tubulin bound to GDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000070biological_processmitotic sister chromatid segregation
A0000212biological_processmeiotic spindle organization
A0000226biological_processmicrotubule cytoskeleton organization
A0000242cellular_componentpericentriolar material
A0000278biological_processmitotic cell cycle
A0000794cellular_componentcondensed nuclear chromosome
A0000930cellular_componentgamma-tubulin complex
A0005200molecular_functionstructural constituent of cytoskeleton
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005814cellular_componentcentriole
A0005819cellular_componentspindle
A0005827cellular_componentpolar microtubule
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0005876cellular_componentspindle microtubule
A0005881cellular_componentcytoplasmic microtubule
A0005929cellular_componentcilium
A0007017biological_processmicrotubule-based process
A0007020biological_processmicrotubule nucleation
A0007052biological_processmitotic spindle organization
A0015630cellular_componentmicrotubule cytoskeleton
A0031122biological_processcytoplasmic microtubule organization
A0031252cellular_componentcell leading edge
A0036064cellular_componentciliary basal body
A0042802molecular_functionidentical protein binding
A0043005cellular_componentneuron projection
A0045177cellular_componentapical part of cell
A0055037cellular_componentrecycling endosome
A0097730cellular_componentnon-motile cilium
A1990498cellular_componentmitotic spindle microtubule
B0000070biological_processmitotic sister chromatid segregation
B0000212biological_processmeiotic spindle organization
B0000226biological_processmicrotubule cytoskeleton organization
B0000242cellular_componentpericentriolar material
B0000278biological_processmitotic cell cycle
B0000794cellular_componentcondensed nuclear chromosome
B0000930cellular_componentgamma-tubulin complex
B0005200molecular_functionstructural constituent of cytoskeleton
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005814cellular_componentcentriole
B0005819cellular_componentspindle
B0005827cellular_componentpolar microtubule
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0005876cellular_componentspindle microtubule
B0005881cellular_componentcytoplasmic microtubule
B0005929cellular_componentcilium
B0007017biological_processmicrotubule-based process
B0007020biological_processmicrotubule nucleation
B0007052biological_processmitotic spindle organization
B0015630cellular_componentmicrotubule cytoskeleton
B0031122biological_processcytoplasmic microtubule organization
B0031252cellular_componentcell leading edge
B0036064cellular_componentciliary basal body
B0042802molecular_functionidentical protein binding
B0043005cellular_componentneuron projection
B0045177cellular_componentapical part of cell
B0055037cellular_componentrecycling endosome
B0097730cellular_componentnon-motile cilium
B1990498cellular_componentmitotic spindle microtubule
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE GDP A 500
ChainResidue
AGLY11
AGLY146
AASN207
APHE225
AILE228
AASN229
AGLN12
ACYS13
AGLN16
AASN102
ASER140
AGLY143
AGLY144
ATHR145

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GDP B 501
ChainResidue
BGLY11
BGLN12
BCYS13
BGLN16
BSER140
BGLY143
BGLY144
BTHR145
BGLY146
BPRO173
BGLU177
BASN207
BPHE225
BILE228
BASN229

Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. AGGTGSG
ChainResidueDetails
AALA142-GLY148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AALA142
BALA142

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine; by BRSK1 => ECO:0000250|UniProtKB:P83887
ChainResidueDetails
ASER131
BSER131

224201

PDB entries from 2024-08-28

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