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6TIU

DROSOPHILA GTP-TUBULIN Y222F MUTANT

Functional Information from GO Data
ChainGOidnamespacecontents
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
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
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
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 Residues23
Detailsbinding site for residue GTP A 501
ChainResidue
AGLY10
ASER140
AGLY143
AGLY144
ATHR145
AGLY146
AVAL177
ATHR179
AGLU183
AASN206
ATYR224
AGLN11
AASN228
AILE231
AMG502
BLYS252
AALA12
AGLN15
AASP69
AASP98
AALA99
AALA100
AASN101

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 502
ChainResidue
AASP69
AGLU71
AGTP501

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

site_idAC4
Number of Residues21
Detailsbinding site for residue GTP B 501
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BALA97
BGLY98
BASN99
BSER138
BGLY141
BGLY142
BTHR143
BGLY144
BPRO171
BVAL175
BGLU181
BASN204
BPHE222
BASN226
BMG502
BGDP503
CGLU254

site_idAC5
Number of Residues3
Detailsbinding site for residue MG B 502
ChainResidue
BGLN11
BTHR72
BGTP501

site_idAC6
Number of Residues17
Detailsbinding site for residue GDP B 503
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BSER138
BGLY141
BGLY142
BTHR143
BGLY144
BSER145
BPRO171
BVAL175
BGLU181
BASN204
BPHE222
BASN226
BGTP501

site_idAC7
Number of Residues3
Detailsbinding site for residue SO4 B 504
ChainResidue
BTHR221
BGLY223
BARG276

site_idAC8
Number of Residues5
Detailsbinding site for residue SO4 B 505
ChainResidue
BLYS216
BLEU217
BTHR218
BTHR219
CLYS326

site_idAC9
Number of Residues23
Detailsbinding site for residue GTP C 600
ChainResidue
CMG601
DLYS252
CGLY10
CGLN11
CALA12
CGLN15
CASP69
CASP98
CALA99
CALA100
CASN101
CSER140
CGLY143
CGLY144
CTHR145
CGLY146
CVAL177
CTHR179
CGLU183
CASN206
CTYR224
CASN228
CILE231

site_idAD1
Number of Residues3
Detailsbinding site for residue MG C 601
ChainResidue
CASP69
CGLU71
CGTP600

site_idAD2
Number of Residues20
Detailsbinding site for residue GTP D 501
ChainResidue
DGLY10
DGLN11
DCYS12
DGLN15
DGLU69
DALA97
DGLY98
DASN99
DSER138
DGLY141
DGLY142
DTHR143
DGLY144
DPRO171
DSER176
DGLU181
DASN204
DPHE222
DASN226
DMG502

site_idAD3
Number of Residues2
Detailsbinding site for residue MG D 502
ChainResidue
DGLN11
DGTP501

site_idAD4
Number of Residues4
Detailsbinding site for residue SO4 D 503
ChainResidue
DTHR221
DGLY223
DARG276
DPHE394

site_idAD5
Number of Residues5
Detailsbinding site for residue SO4 D 504
ChainResidue
DLYS19
DHIS227
DSER230
DARG276
DARG359

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 Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ESER46
DGLY142
DTHR143
DGLY144
DASN204
DASN226
BSER138
BGLY142
BTHR143
BGLY144
BASN204
BASN226
DGLN11
DSER138

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
BGLU69
CGLU71
CSER140
CGLY144
CTHR145
CTHR179
CASN206
CASN228
DGLU69
ASER140
AGLY144
ATHR145
ATHR179
AASN206
AASN228
CGLN11

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:18327897
ChainResidueDetails
BSER40
BSER339
DSER40
DSER339

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:36342916
ChainResidueDetails
AARG40
CARG40

226707

PDB entries from 2024-10-30

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