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4ZOL

Crystal Structure of Tubulin-Stathmin-TTL-Tubulysin M 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 Residues27
DetailsBINDING SITE FOR RESIDUE GTP A 501
ChainResidue
AGLY10
AGLY144
ATHR145
AGLY146
AVAL177
AGLU183
AASN206
ATYR224
AASN228
AILE231
AMG502
AGLN11
AHOH615
AHOH623
AHOH632
AHOH634
AHOH646
AHOH653
AHOH655
BLYS254
AALA12
AGLN15
AASP98
AALA99
AASN101
ASER140
AGLY143

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AGTP501
AHOH623
AHOH632
AHOH634
AHOH646
BLYS254

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 503
ChainResidue
AASP39
ATHR41
AGLY44
AGLU55
AHOH603

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 504
ChainResidue
ASER158
AGLY162
ALYS166
AGLU196
AASP199
AHOH619
EASP44

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 505
ChainResidue
AASN216
APRO274
AVAL275
AILE276
AASN300
AHOH641

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 506
ChainResidue
AALA208
AASP211
AILE212
AARG215
APRO298
AALA299
AGLN301
ALYS304
FGOL402

site_idAC7
Number of Residues23
DetailsBINDING SITE FOR RESIDUE GDP B 501
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BSER140
BGLY143
BGLY144
BTHR145
BGLY146
BVAL177
BSER178
BGLU183
BASN206
BTYR224
BASN228
BMG502
B55Q507
BHOH601
BHOH606
BHOH607
BHOH613
BHOH620
BHOH628

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 502
ChainResidue
BGLU71
BGDP501
BHOH620
BHOH629
BHOH655
BHOH663

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MES B 503
ChainResidue
BPHE296
BASP297
BALA298
BARG308
BASN339
BTYR342

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MES B 504
ChainResidue
BASN197
BTHR198
BASP199
BARG253
BHOH615
BARG158
BASP163
BARG164
BILE165

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 505
ChainResidue
BASP116
BASP120
CASP218
CGLU220

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 506
ChainResidue
BARG401
CGLU434
CGOL504

site_idBC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 55Q B 507
ChainResidue
BGLN15
BLYS176
BASP179
BPRO222
BTHR223
BTYR224
BGLY225
BARG278
BGDP501
BHOH609
BHOH618
CASN329
CVAL353

site_idBC5
Number of Residues26
DetailsBINDING SITE FOR RESIDUE GTP C 501
ChainResidue
CGLY10
CGLN11
CALA12
CGLN15
CASP98
CALA99
CASN101
CSER140
CGLY143
CGLY144
CTHR145
CGLY146
CVAL177
CGLU183
CASN206
CTYR224
CASN228
CILE231
CMG502
CHOH606
CHOH609
CHOH627
CHOH633
CHOH662
CHOH668
DLYS254

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 502
ChainResidue
CGTP501
CHOH606
CHOH609
CHOH633
CHOH662

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 503
ChainResidue
CASP39
CTHR41
CGLY44
CGLU55
CHOH602

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL C 504
ChainResidue
BGOL506
CASP431
CHOH678

site_idBC9
Number of Residues23
DetailsBINDING SITE FOR RESIDUE GDP D 501
ChainResidue
DGLY10
DGLN11
DCYS12
DGLN15
DSER140
DGLY143
DGLY144
DTHR145
DGLY146
DVAL177
DSER178
DGLU183
DASN206
DTYR224
DLEU227
DASN228
DMG502
DHOH601
DHOH607
DHOH609
DHOH620
DHOH624
DHOH629

site_idCC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 502
ChainResidue
DGDP501
DHOH601
DHOH604
DHOH607
DHOH609
DHOH629

site_idCC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 55Q D 503
ChainResidue
DGLN15
DPRO175
DLYS176
DVAL177
DASP179
DPRO222
DTHR223
DTYR224
DGLY225
DARG278

site_idCC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ACP F 401
ChainResidue
FLYS74
FILE148
FLYS150
FGLN183
FLYS184
FTYR185
FLEU186
FLYS198
FASP200
FARG222
FLEU240
FTHR241
FASN242
FASP318
FGLU331
FASN333
FHOH501

site_idCC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL F 402
ChainResidue
AARG215
AGOL506
FHIS306
FLEU307
FHIS308

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: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
BLYS60
DLYS60

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885
ChainResidueDetails
BSER174
DSER174
CSER48
CSER232

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

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
BLYS60
DLYS60

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
BLYS326
DLYS326

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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