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6TIS

DROSOPHILA GDP-TUBULIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000226biological_processmicrotubule cytoskeleton organization
A0000235cellular_componentastral microtubule
A0000278biological_processmitotic cell cycle
A0005200molecular_functionstructural constituent of cytoskeleton
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005819cellular_componentspindle
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0007017biological_processmicrotubule-based process
A0016787molecular_functionhydrolase activity
A0032418biological_processlysosome localization
A0046872molecular_functionmetal ion binding
A0048471cellular_componentperinuclear region of cytoplasm
B0000166molecular_functionnucleotide binding
B0000226biological_processmicrotubule cytoskeleton organization
B0000278biological_processmitotic cell cycle
B0003924molecular_functionGTPase activity
B0005200molecular_functionstructural constituent of cytoskeleton
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0007017biological_processmicrotubule-based process
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0000226biological_processmicrotubule cytoskeleton organization
C0000235cellular_componentastral microtubule
C0000278biological_processmitotic cell cycle
C0005200molecular_functionstructural constituent of cytoskeleton
C0005525molecular_functionGTP binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005813cellular_componentcentrosome
C0005819cellular_componentspindle
C0005856cellular_componentcytoskeleton
C0005874cellular_componentmicrotubule
C0007017biological_processmicrotubule-based process
C0016787molecular_functionhydrolase activity
C0032418biological_processlysosome localization
C0046872molecular_functionmetal ion binding
C0048471cellular_componentperinuclear region of cytoplasm
D0000166molecular_functionnucleotide binding
D0000226biological_processmicrotubule cytoskeleton organization
D0000278biological_processmitotic cell cycle
D0003924molecular_functionGTPase activity
D0005200molecular_functionstructural constituent of cytoskeleton
D0005525molecular_functionGTP binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005874cellular_componentmicrotubule
D0007017biological_processmicrotubule-based process
D0046872molecular_functionmetal ion binding
E0031110biological_processregulation of microtubule polymerization or depolymerization
Functional Information from PDB Data
site_idAC1
Number of Residues27
Detailsbinding site for residue GTP A 501
ChainResidue
AGLY10
AGLY144
ATHR145
AGLY146
AVAL177
ATHR179
AGLU183
AASN206
ATYR224
AASN228
AILE231
AGLN11
AMG502
AHOH625
AHOH627
AHOH636
AHOH668
AHOH673
AHOH686
BLYS252
AALA12
AGLN15
AASP98
AALA99
AASN101
ASER140
AGLY143

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 502
ChainResidue
AGTP501
AHOH617
AHOH636
AHOH673
AHOH686

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 503
ChainResidue
APRO175
ALYS394
BASN347

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 504
ChainResidue
AARG308
AARG339
ATHR340
AHOH611

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 A 505
ChainResidue
AASN216
AVAL275
AHOH621

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 A 506
ChainResidue
AVAL177
AARG221
ATYR224

site_idAC7
Number of Residues5
Detailsbinding site for residue GOL A 507
ChainResidue
AARG105
AGLY410
AGLU411
EARG61
EGLU65

site_idAC8
Number of Residues18
Detailsbinding site for residue GDP B 501
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BSER138
BGLY141
BGLY142
BTHR143
BGLY144
BVAL175
BGLU181
BASN204
BTYR222
BASN226
BHOH604
BHOH617
BHOH619
BHOH644

site_idAC9
Number of Residues3
Detailsbinding site for residue SO4 B 502
ChainResidue
BTHR221
BGLY223
BARG276

site_idAD1
Number of Residues5
Detailsbinding site for residue SO4 B 503
ChainResidue
BLYS216
BLEU217
BTHR218
BTHR219
CLYS326

site_idAD2
Number of Residues6
Detailsbinding site for residue SO4 B 504
ChainResidue
BLYS336
BASN337
BSER338
BSER339
BHOH665
DLYS297

site_idAD3
Number of Residues6
Detailsbinding site for residue GOL B 505
ChainResidue
BPRO173
BLYS174
BSER176
BHOH671
CASN329
CLYS336

site_idAD4
Number of Residues26
Detailsbinding site for residue GTP C 501
ChainResidue
CGLY146
CVAL177
CTHR179
CGLU183
CASN206
CTYR224
CASN228
CILE231
CMG502
CHOH610
CHOH612
CHOH617
CHOH620
CHOH680
DLYS252
CGLY10
CGLN11
CALA12
CGLN15
CASP98
CALA99
CASN101
CSER140
CGLY143
CGLY144
CTHR145

site_idAD5
Number of Residues5
Detailsbinding site for residue MG C 502
ChainResidue
CGTP501
CHOH610
CHOH612
CHOH617
CHOH680

site_idAD6
Number of Residues3
Detailsbinding site for residue SO4 C 503
ChainResidue
CPRO175
CLYS394
DASN347

site_idAD7
Number of Residues20
Detailsbinding site for residue GDP D 501
ChainResidue
DGLY10
DGLN11
DCYS12
DGLN15
DSER138
DGLY141
DGLY142
DTHR143
DGLY144
DVAL175
DGLU181
DASN204
DTYR222
DASN226
DHOH607
DHOH620
DHOH625
DHOH626
DHOH628
DHOH653

site_idAD8
Number of Residues4
Detailsbinding site for residue SO4 D 502
ChainResidue
DTHR221
DARG276
DHOH601
DHOH608

site_idAD9
Number of Residues6
Detailsbinding site for residue SO4 D 503
ChainResidue
DALA271
DPRO272
DLEU273
DLEU284
DASN298
DHOH666

site_idAE1
Number of Residues6
Detailsbinding site for residue SO4 D 504
ChainResidue
DLYS19
DHIS227
DARG276
DARG359
DHOH617
DHOH670

Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
BGLY140-GLY146
AGLY142-GLY148

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

site_idPS00563
Number of Residues10
DetailsSTATHMIN_1 Stathmin family signature 1. PRRRDpSLEE
ChainResidueDetails
EPRO40-GLU49

site_idPS01041
Number of Residues10
DetailsSTATHMIN_2 Stathmin family signature 2. AEKREHEREV
ChainResidueDetails
EALA73-VAL82

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18327897","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues21
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues99
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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