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5JQG

An apo tubulin-RB-TTL complex structure used for side-by-side comparison

Functional Information from GO Data
ChainGOidnamespacecontents
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0003924molecular_functionGTPase activity
A0005200molecular_functionstructural constituent of cytoskeleton
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0007017biological_processmicrotubule-based process
A0015630cellular_componentmicrotubule cytoskeleton
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
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
B0007017biological_processmicrotubule-based process
B0046872molecular_functionmetal ion binding
C0000226biological_processmicrotubule cytoskeleton organization
C0000278biological_processmitotic cell cycle
C0003924molecular_functionGTPase activity
C0005200molecular_functionstructural constituent of cytoskeleton
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0005874cellular_componentmicrotubule
C0007017biological_processmicrotubule-based process
C0015630cellular_componentmicrotubule cytoskeleton
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
D0000226biological_processmicrotubule cytoskeleton organization
D0000278biological_processmitotic cell cycle
D0003924molecular_functionGTPase activity
D0005200molecular_functionstructural constituent of cytoskeleton
D0005515molecular_functionprotein binding
D0005525molecular_functionGTP binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005874cellular_componentmicrotubule
D0007017biological_processmicrotubule-based process
D0046872molecular_functionmetal ion binding
E0031110biological_processregulation of microtubule polymerization or depolymerization
F0036211biological_processprotein modification process
Functional Information from PDB Data
site_idAC1
Number of Residues29
Detailsbinding site for residue GTP A 501
ChainResidue
AGLY10
AGLY143
AGLY144
ATHR145
AGLY146
AVAL177
ATHR179
AGLU183
AASN206
ATYR224
AASN228
AGLN11
AILE231
AMG502
AHOH609
AHOH615
AHOH616
AHOH633
AHOH643
AHOH645
AHOH647
BLYS252
AALA12
AGLN15
AASP98
AALA99
AALA100
AASN101
ASER140

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 502
ChainResidue
AGTP501
AHOH616
AHOH633
AHOH645
AHOH647

site_idAC3
Number of Residues5
Detailsbinding site for residue CA A 503
ChainResidue
AASP39
ATHR41
AGLY44
AGLU55
AHOH603

site_idAC4
Number of Residues4
Detailsbinding site for residue CL A 504
ChainResidue
ATYR161
AGLY162
ALYS163
ALYS164

site_idAC5
Number of Residues25
Detailsbinding site for residue GDP B 501
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BSER138
BGLY141
BGLY142
BTHR143
BGLY144
BPRO171
BVAL175
BASP177
BGLU181
BASN204
BTYR222
BASN226
BMG502
BHOH601
BHOH606
BHOH609
BHOH612
BHOH623
BHOH631
BHOH643
BHOH653

site_idAC6
Number of Residues6
Detailsbinding site for residue MG B 502
ChainResidue
BGLN11
BGDP501
BHOH602
BHOH643
BHOH653
CHOH627

site_idAC7
Number of Residues1
Detailsbinding site for residue CA B 503
ChainResidue
BGLU111

site_idAC8
Number of Residues8
Detailsbinding site for residue MES B 504
ChainResidue
ATRP407
BARG156
BPRO160
BASP161
BARG162
BASN195
BASP197
BARG251

site_idAC9
Number of Residues7
Detailsbinding site for residue MES B 505
ChainResidue
BPHE294
BASP295
BALA296
BASP304
BARG306
BASN337
BHOH608

site_idAD1
Number of Residues28
Detailsbinding site for residue GTP C 501
ChainResidue
CGLY143
CGLY144
CTHR145
CGLY146
CVAL177
CGLU183
CASN206
CTYR224
CASN228
CILE231
CMG502
CHOH607
CHOH610
CHOH633
CHOH644
CHOH645
CHOH676
CHOH692
DLYS252
CGLY10
CGLN11
CALA12
CGLN15
CASP98
CALA99
CALA100
CASN101
CSER140

site_idAD2
Number of Residues5
Detailsbinding site for residue MG C 502
ChainResidue
CGTP501
CHOH607
CHOH633
CHOH645
CHOH692

site_idAD3
Number of Residues5
Detailsbinding site for residue CA C 503
ChainResidue
CASP39
CTHR41
CGLY44
CGLU55
CHOH615

site_idAD4
Number of Residues22
Detailsbinding site for residue GTP D 501
ChainResidue
DGLY10
DGLN11
DCYS12
DGLN15
DALA97
DGLY98
DASN99
DSER138
DGLY141
DGLY142
DTHR143
DGLY144
DGLU181
DASN204
DTYR222
DASN226
DMG502
DHOH601
DHOH605
DHOH607
DHOH613
DHOH622

site_idAD5
Number of Residues4
Detailsbinding site for residue MG D 502
ChainResidue
DGTP501
DHOH601
DHOH605
DHOH629

site_idAD6
Number of Residues17
Detailsbinding site for residue ACP F 401
ChainResidue
FLYS74
FILE148
FLYS150
FGLN183
FLYS184
FTYR185
FLEU186
FLYS198
FASP200
FARG202
FARG222
FTHR241
FASN242
FASP318
FILE330
FGLU331
FASN333

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

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 Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
BSER40
DSER40

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
BLYS58
DLYS58

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885
ChainResidueDetails
BSER172
DSER172
CSER48
CSER232

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BTHR285
BTHR290
DTHR285
DTHR290

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BARG318
DARG318

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q2T9S0
ChainResidueDetails
BGLU438
DGLU438

site_idSWS_FT_FI9
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BLYS58
DLYS58

site_idSWS_FT_FI10
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
AGLU445
BLYS324
DLYS324

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:Q71U36
ChainResidueDetails
ATYR451
CTYR451

site_idSWS_FT_FI12
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
ALYS326
ALYS370
CLYS326
CLYS370

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PDB entries from 2024-07-24

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