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4O4I

Tubulin-Laulimalide-Epothilone A complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0003725molecular_functiondouble-stranded RNA binding
A0003924molecular_functionGTPase activity
A0005200molecular_functionstructural constituent of cytoskeleton
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0005881cellular_componentcytoplasmic microtubule
A0005929cellular_componentcilium
A0007017biological_processmicrotubule-based process
A0015630cellular_componentmicrotubule cytoskeleton
A0016787molecular_functionhydrolase activity
A0031625molecular_functionubiquitin protein ligase binding
A0046872molecular_functionmetal ion binding
A0071353biological_processcellular response to interleukin-4
B0000166molecular_functionnucleotide binding
B0000226biological_processmicrotubule cytoskeleton organization
B0000278biological_processmitotic cell cycle
B0001764biological_processneuron migration
B0003924molecular_functionGTPase activity
B0005200molecular_functionstructural constituent of cytoskeleton
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0007017biological_processmicrotubule-based process
B0007399biological_processnervous system development
B0015630cellular_componentmicrotubule cytoskeleton
B0046872molecular_functionmetal ion binding
B0046982molecular_functionprotein heterodimerization activity
B1902669biological_processpositive regulation of axon guidance
C0000166molecular_functionnucleotide binding
C0000226biological_processmicrotubule cytoskeleton organization
C0000278biological_processmitotic cell cycle
C0003725molecular_functiondouble-stranded RNA binding
C0003924molecular_functionGTPase activity
C0005200molecular_functionstructural constituent of cytoskeleton
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0005874cellular_componentmicrotubule
C0005881cellular_componentcytoplasmic microtubule
C0005929cellular_componentcilium
C0007017biological_processmicrotubule-based process
C0015630cellular_componentmicrotubule cytoskeleton
C0016787molecular_functionhydrolase activity
C0031625molecular_functionubiquitin protein ligase binding
C0046872molecular_functionmetal ion binding
C0071353biological_processcellular response to interleukin-4
D0000166molecular_functionnucleotide binding
D0000226biological_processmicrotubule cytoskeleton organization
D0000278biological_processmitotic cell cycle
D0001764biological_processneuron migration
D0003924molecular_functionGTPase activity
D0005200molecular_functionstructural constituent of cytoskeleton
D0005525molecular_functionGTP binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005874cellular_componentmicrotubule
D0007017biological_processmicrotubule-based process
D0007399biological_processnervous system development
D0015630cellular_componentmicrotubule cytoskeleton
D0046872molecular_functionmetal ion binding
D0046982molecular_functionprotein heterodimerization activity
D1902669biological_processpositive regulation of axon guidance
E0031110biological_processregulation of microtubule polymerization or depolymerization
F0036211biological_processprotein modification process
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE GTP A 501
ChainResidue
AGLY10
AGLY143
AGLY144
ATHR145
AGLY146
AVAL177
AGLU183
AASN206
ATYR224
AASN228
AILE231
AGLN11
AMG502
AHOH603
AHOH604
AHOH611
AHOH706
BLYS254
AALA12
AGLN15
AASP98
AALA99
AALA100
AASN101
ASER140

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AGLU71
AGTP501
AHOH603
AHOH704
AHOH706

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 503
ChainResidue
AASP39
ATHR41
AGLY44
AGLY45
AGLU55

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP B 501
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BSER140
BGLY143
BGLY144
BTHR145
BGLY146
BVAL177
BASP179
BGLU183
BASN206
BTYR224
BASN228
BMG502
BMG504
BHOH601
BHOH605
BHOH606
BHOH615

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 502
ChainResidue
BGLU71
BGDP501
BMG504
BHOH685

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE EP B 503
ChainResidue
BLEU217
BLEU219
BASP226
BHIS229
BALA233
BPHE272
BPRO274
BLEU275
BTHR276
BARG278
BGLN281
BGLN282
BARG284
BLEU371

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 504
ChainResidue
BGLN11
BASP179
BGDP501
BMG502
BHOH684
CHOH618

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE LLM B 505
ChainResidue
BGLN293
BPHE296
BASP297
BSER298
BARG308
BASN334
BASN339
BHOH622

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA B 506
ChainResidue
BGLU113

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MES B 507
ChainResidue
BARG158
BPRO162
BASP163
BARG164
BASN197
BTHR198
BASP199
BARG253
BHOH650

site_idBC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE GTP C 501
ChainResidue
CGLN11
CALA12
CGLN15
CASP98
CALA99
CALA100
CASN101
CSER140
CGLY143
CGLY144
CTHR145
CGLY146
CVAL177
CGLU183
CASN206
CTYR224
CASN228
CILE231
CMG502
CHOH603
CHOH604
CHOH606
CHOH752
DLYS254
CGLY10

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG C 502
ChainResidue
CGTP501
CHOH602
CHOH604
CHOH606

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 503
ChainResidue
CASP39
CTHR41
CGLY44
CGLY45
CGLU55

site_idBC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GDP D 501
ChainResidue
DGLY10
DGLN11
DCYS12
DGLN15
DSER140
DGLY143
DGLY144
DTHR145
DGLY146
DSER178
DGLU183
DASN206
DTYR224
DASN228
DMG502
DHOH604
DHOH660

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG D 502
ChainResidue
DGLN11
DGDP501

site_idBC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EP D 503
ChainResidue
DLEU217
DASP226
DHIS229
DPRO274
DLEU275
DTHR276
DARG278
DGLN281

site_idBC8
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ACP F 500
ChainResidue
FLYS74
FILE148
FLYS150
FGLN183
FLYS184
FTYR185
FLEU186
FLYS198
FTHR241
FASN242
FASP318
FILE330
FGLU331
FASN333
FMG501

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG F 501
ChainResidue
FARG202
FARG222
FASP318
FGLU331
FACP500

Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
AGLY142-GLY148
BGLY142-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
DGLY144
DTHR145
DGLY146
DASN206
DASN228
BSER140
BGLY144
BTHR145
BGLY146
BASN206
BASN228
DGLN11
DSER140

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
BGLU71
CGLU71
CSER140
CGLY144
CTHR145
CTHR179
CASN206
CASN228
DGLU71
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: Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8
ChainResidueDetails
BTHR57
DTHR57

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
BLYS60
DLYS60
CSER48
CSER232

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1
ChainResidueDetails
BSER174
DSER174

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BTHR287
BTHR292
DTHR287
DTHR292

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BARG320
DARG320

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q2T9S0
ChainResidueDetails
BGLU448
DGLU448

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BLYS60
DLYS60

site_idSWS_FT_FI11
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
ATYR451
BLYS326
DLYS326

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 2025-06-11

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