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4YJ2

Crystal structure of tubulin bound to MI-181

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0003924molecular_functionGTPase activity
A0005200molecular_functionstructural constituent of cytoskeleton
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0007017biological_processmicrotubule-based process
A0015630cellular_componentmicrotubule cytoskeleton
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
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
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
C0003924molecular_functionGTPase activity
C0005200molecular_functionstructural constituent of cytoskeleton
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0005874cellular_componentmicrotubule
C0007017biological_processmicrotubule-based process
C0015630cellular_componentmicrotubule cytoskeleton
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
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
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 Residues27
Detailsbinding site for residue GTP A 501
ChainResidue
AGLY10
AGLY143
AGLY144
ATHR145
AGLY146
AVAL177
ASER178
AGLU183
AASN206
ATYR224
AASN228
AGLN11
AILE231
AMG502
AHOH604
AHOH610
AHOH611
AHOH615
AHOH618
BLYS254
AALA12
AGLN15
AASP98
AALA99
AALA100
AASN101
ASER140

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 502
ChainResidue
AGLU71
AGTP501
AHOH604
AHOH611
AHOH615
AHOH618

site_idAC3
Number of Residues5
Detailsbinding site for residue CA A 503
ChainResidue
AASP39
ATHR41
AGLY44
AGLU55
AHOH601

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 504
ChainResidue
AASN216
APRO274
AVAL275
AALA294
AASN300

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL A 505
ChainResidue
AHIS309
ATHR382
AALA383
AGLU386
FARG66

site_idAC6
Number of Residues22
Detailsbinding site for residue GDP B 501
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BSER140
BGLY143
BGLY144
BTHR145
BGLY146
BVAL177
BASP179
BGLU183
BASN206
BTYR224
BASN228
BMG502
BHOH603
BHOH604
BHOH606
BHOH609
BHOH620
BHOH621

site_idAC7
Number of Residues6
Detailsbinding site for residue MG B 502
ChainResidue
BGLN11
BGDP501
BHOH605
BHOH621
BHOH626
CHOH632

site_idAC8
Number of Residues4
Detailsbinding site for residue CA B 503
ChainResidue
BGLU113
BHOH613
CHOH635
CHOH647

site_idAC9
Number of Residues13
Detailsbinding site for residue 4ED B 504
ChainResidue
BGLN136
BASN167
BGLU200
BTYR202
BVAL238
BTHR239
BCYS241
BLEU242
BLEU252
BLEU255
BALA316
BILE318
BHOH602

site_idAD1
Number of Residues7
Detailsbinding site for residue MES B 505
ChainResidue
BARG253
BARG158
BASP163
BARG164
BILE165
BASN197
BASP199

site_idAD2
Number of Residues9
Detailsbinding site for residue MES B 506
ChainResidue
BPHE296
BASP297
BSER298
BARG308
BTYR312
BVAL335
BASN339
BTYR342
BHOH601

site_idAD3
Number of Residues3
Detailsbinding site for residue GOL B 507
ChainResidue
BPRO222
BTYR224
BHOH629

site_idAD4
Number of Residues29
Detailsbinding site for residue GTP C 501
ChainResidue
CGLY10
CGLN11
CALA12
CGLN15
CASP69
CASP98
CALA99
CALA100
CASN101
CSER140
CGLY143
CGLY144
CTHR145
CGLY146
CILE171
CVAL177
CGLU183
CASN206
CTYR224
CASN228
CILE231
CMG505
CHOH611
CHOH612
CHOH620
CHOH622
CHOH629
CHOH637
DLYS254

site_idAD5
Number of Residues5
Detailsbinding site for residue CA C 502
ChainResidue
CASP39
CTHR41
CGLY44
CGLU55
CHOH609

site_idAD6
Number of Residues4
Detailsbinding site for residue GOL C 503
ChainResidue
CARG221
CTHR223
CTYR224
DGLN247

site_idAD7
Number of Residues2
Detailsbinding site for residue IMD C 504
ChainResidue
CASP431
CHOH643

site_idAD8
Number of Residues5
Detailsbinding site for residue MG C 505
ChainResidue
CGTP501
CHOH611
CHOH620
CHOH629
CHOH637

site_idAD9
Number of Residues17
Detailsbinding site for residue GDP D 501
ChainResidue
DGLY10
DGLN11
DCYS12
DGLN15
DASN101
DSER140
DGLY143
DGLY144
DTHR145
DGLY146
DVAL177
DGLU183
DASN206
DTYR224
DASN228
DMG502
DHOH605

site_idAE1
Number of Residues5
Detailsbinding site for residue MG D 502
ChainResidue
DGLN11
DASP179
DGDP501
DHOH602
DHOH608

site_idAE2
Number of Residues18
Detailsbinding site for residue 4ED D 503
ChainResidue
DGLN136
DASN167
DPHE169
DGLU200
DTYR202
DVAL238
DTHR239
DCYS241
DLEU242
DLEU248
DASN249
DLEU252
DLEU255
DALA316
DILE318
DALA354
DILE378
DHOH607

site_idAE3
Number of Residues7
Detailsbinding site for residue GOL D 504
ChainResidue
CTRP407
DARG158
DASP163
DARG164
DILE165
DASP199
DARG253

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
ESER19
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

218853

PDB entries from 2024-04-24

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