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6LSN

Crystal structure of tubulin-inhibitor complex

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 Residues25
Detailsbinding site for residue GTP A 501
ChainResidue
AGLY10
AGLY143
AGLY144
ATHR145
AGLY146
AILE171
AVAL177
ASER178
AGLU183
AASN206
ATYR224
AGLN11
AASN228
AILE231
AMG502
AHOH619
AHOH629
BLYS254
AALA12
AGLN15
AASP98
AALA99
AALA100
AASN101
ASER140

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 502
ChainResidue
AGTP501
AHOH612
AHOH619

site_idAC3
Number of Residues4
Detailsbinding site for residue CA A 503
ChainResidue
AASP39
ATHR41
AGLY44
AGLU55

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

site_idAC5
Number of Residues2
Detailsbinding site for residue CA A 505
ChainResidue
AHOH606
EHOH213

site_idAC6
Number of Residues21
Detailsbinding site for residue GDP B 501
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BSER140
BGLY143
BGLY144
BTHR145
BGLY146
BPRO173
BVAL177
BASP179
BGLU183
BASN206
BTYR224
BASN228
BMG502
BHOH604
BHOH620
BHOH629
BHOH634

site_idAC7
Number of Residues6
Detailsbinding site for residue MG B 502
ChainResidue
BGLN11
BGDP501
BHOH611
BHOH637
BHOH646
BHOH649

site_idAC8
Number of Residues1
Detailsbinding site for residue CA B 503
ChainResidue
BGLU113

site_idAC9
Number of Residues8
Detailsbinding site for residue MES B 504
ChainResidue
BARG158
BPRO162
BASP163
BARG164
BASN197
BTHR198
BASP199
BARG253

site_idAD1
Number of Residues6
Detailsbinding site for residue MES B 505
ChainResidue
BPHE296
BASP297
BSER298
BARG308
BASN339
BTYR342

site_idAD2
Number of Residues3
Detailsbinding site for residue MG B 506
ChainResidue
BHOH608
CGLU220
CHOH721

site_idAD3
Number of Residues17
Detailsbinding site for residue ERR B 507
ChainResidue
BHOH636
ATHR179
AVAL181
BVAL238
BCYS241
BLEU242
BLEU248
BASN249
BLYS254
BASN258
BVAL315
BALA316
BILE318
BASN349
BASN350
BLYS352
BILE378

site_idAD4
Number of Residues26
Detailsbinding site for residue GTP C 501
ChainResidue
CGLY10
CGLN11
CALA12
CGLN15
CASP98
CALA99
CALA100
CASN101
CSER140
CGLY143
CGLY144
CTHR145
CGLY146
CILE171
CVAL177
CGLU183
CASN206
CTYR224
CASN228
CILE231
CMG502
CHOH621
CHOH622
CHOH645
CHOH671
DLYS254

site_idAD5
Number of Residues6
Detailsbinding site for residue MG C 502
ChainResidue
CGLU71
CGTP501
CHOH621
CHOH622
CHOH671
DLYS254

site_idAD6
Number of Residues5
Detailsbinding site for residue CA C 503
ChainResidue
CASP39
CTHR41
CGLY44
CGLU55
CHOH612

site_idAD7
Number of Residues14
Detailsbinding site for residue GDP D 600
ChainResidue
DGLY10
DGLN11
DCYS12
DSER140
DGLY143
DGLY144
DTHR145
DGLY146
DSER178
DGLU183
DASN206
DTYR224
DASN228
DMG601

site_idAD8
Number of Residues2
Detailsbinding site for residue MG D 601
ChainResidue
DGLN11
DGDP600

site_idAD9
Number of Residues4
Detailsbinding site for residue MG F 401
ChainResidue
FLYS74
FGLU331
FASN333
FACP402

site_idAE1
Number of Residues18
Detailsbinding site for residue ACP F 402
ChainResidue
FLYS74
FILE148
FGLN183
FLYS184
FTYR185
FLEU186
FLYS198
FASP200
FARG202
FARG222
FHIS239
FTHR241
FASN242
FASP318
FMET320
FGLU331
FASN333
FMG401

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 Residues14
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q13509
ChainResidueDetails
BGLY144
BTHR145
BGLY146
BASN206
BASN228
DGLN11
DSER140
DGLY144
DTHR145
DGLY146
DASN206
DASN228
BGLN11
BSER140

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
ASER140
AGLY144
ATHR145
ATHR179
AASN206
AASN228
CGLN11
CGLU71
CSER140
CGLY144
CTHR145
CTHR179
CASN206
CASN228
BGLU71
DGLU71

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
CSER48
CSER232
BLYS60
DLYS60

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885
ChainResidueDetails
BSER174
DSER174

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
DTHR287
DTHR292
BTHR287
BTHR292

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BARG320
DARG320

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q2T9S0
ChainResidueDetails
BGLU448
DGLU448

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
DLYS60
BLYS60

site_idSWS_FT_FI10
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
ALYS326
ALYS370
DLYS326
CLYS370
BLYS326

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PDB entries from 2024-06-12

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