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5BMV

CRYSTAL STRUCTURE OF TUBULIN-STATHMIN-TTL-Vinblastine COMPLEX

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
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0007017biological_processmicrotubule-based process
B0046872molecular_functionmetal ion binding
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
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
AGLY143
AGLY144
ATHR145
AGLY146
AVAL177
AGLU183
AASN206
ATYR224
AASN228
AILE231
AGLN11
AMG502
AHOH605
AHOH608
AHOH609
AHOH616
AHOH623
AHOH631
BLYS254
AALA12
AGLN15
AASP98
AALA99
AALA100
AASN101
ASER140

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 502
ChainResidue
AGTP501
AHOH605
AHOH608
AHOH609
AHOH631

site_idAC3
Number of Residues5
Detailsbinding site for residue CA A 503
ChainResidue
AASP39
ATHR41
AGLY44
AGLU55
AHOH624

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 504
ChainResidue
ALYS164
ALYS166
AGLU196
AASP199
EASP44

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL A 505
ChainResidue
AASN216
AVAL275
AILE276
AALA294
AASN300

site_idAC6
Number of Residues2
Detailsbinding site for residue GOL A 506
ChainResidue
AARG221
ATYR224

site_idAC7
Number of Residues24
Detailsbinding site for residue GDP B 501
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BSER140
BGLY143
BGLY144
BTHR145
BGLY146
BPRO173
BVAL177
BGLU183
BASN206
BTYR224
BASN228
BMG502
BHOH601
BHOH604
BHOH618
BHOH620
BHOH622
BHOH633
BHOH634
BHOH641

site_idAC8
Number of Residues5
Detailsbinding site for residue MG B 502
ChainResidue
BGLN11
BGDP501
BHOH604
BHOH622
BHOH653

site_idAC9
Number of Residues2
Detailsbinding site for residue CA B 503
ChainResidue
BGLU113
BHOH651

site_idAD1
Number of Residues6
Detailsbinding site for residue MES B 504
ChainResidue
BARG158
BASP163
BARG164
BASN197
BASP199
BARG253

site_idAD2
Number of Residues8
Detailsbinding site for residue MES B 505
ChainResidue
BPHE296
BASP297
BALA298
BARG308
BVAL335
BASN339
BTYR342
BHOH605

site_idAD3
Number of Residues3
Detailsbinding site for residue GOL B 506
ChainResidue
BARG401
CGLU434
CGOL506

site_idAD4
Number of Residues28
Detailsbinding site for residue GTP C 501
ChainResidue
CALA12
CGLN15
CASP98
CALA99
CALA100
CASN101
CSER140
CGLY143
CGLY144
CTHR145
CGLY146
CVAL177
CTHR179
CGLU183
CASN206
CTYR224
CASN228
CMG502
CHOH609
CHOH613
CHOH627
CHOH649
CHOH653
CHOH655
CHOH662
DLYS254
CGLY10
CGLN11

site_idAD5
Number of Residues5
Detailsbinding site for residue MG C 502
ChainResidue
CGTP501
CHOH613
CHOH627
CHOH649
CHOH662

site_idAD6
Number of Residues5
Detailsbinding site for residue CA C 503
ChainResidue
CASP39
CTHR41
CGLY44
CGLU55
CHOH645

site_idAD7
Number of Residues5
Detailsbinding site for residue GOL C 504
ChainResidue
CASP205
CGLU207
CLYS304
CARG390
CHOH634

site_idAD8
Number of Residues6
Detailsbinding site for residue GOL C 505
ChainResidue
CALA19
CGLU22
CARG229
CSER232
CVAL363
CHOH665

site_idAD9
Number of Residues3
Detailsbinding site for residue GOL C 506
ChainResidue
BGOL506
CASP431
CHOH641

site_idAE1
Number of Residues14
Detailsbinding site for residue VLB C 507
ChainResidue
BPRO175
BLYS176
BVAL177
BASP179
BTYR210
BPHE214
BTHR220
BPRO222
BTHR223
BLEU227
CPRO325
CASN329
CPHE351
CVAL353

site_idAE2
Number of Residues17
Detailsbinding site for residue GDP D 501
ChainResidue
DGLY10
DGLN11
DCYS12
DGLN15
DSER140
DGLY143
DGLY144
DTHR145
DGLY146
DVAL177
DSER178
DGLU183
DASN206
DTYR224
DASN228
DMG502
DHOH603

site_idAE3
Number of Residues1
Detailsbinding site for residue MG D 502
ChainResidue
DGDP501

site_idAE4
Number of Residues16
Detailsbinding site for residue ACP F 401
ChainResidue
FLYS74
FILE148
FGLN183
FLYS184
FLEU186
FLYS198
FASP200
FARG202
FARG222
FHIS239
FLEU240
FTHR241
FASN242
FASP318
FGLU331
FASN333

Functional Information from PROSITE/UniProt
site_idPS00563
Number of Residues10
DetailsSTATHMIN_1 Stathmin family signature 1. PRRRDpSLEE
ChainResidueDetails
EPRO40-GLU49

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_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

218853

PDB entries from 2024-04-24

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