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5ZXH

The structure of MT189-tubulin 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
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
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 Residues23
Detailsbinding site for residue GTP A 501
ChainResidue
AGLY10
AGLY144
ATHR145
AGLY146
AVAL177
AGLU183
AASN206
ATYR224
AASN228
AILE231
AMG502
AGLN11
AHOH603
AHOH604
AHOH606
BLYS252
AALA12
AGLN15
AASP98
AALA99
AASN101
ASER140
AGLY143

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 502
ChainResidue
AGTP501
AHOH602
AHOH604
AHOH606
BHOH601

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

site_idAC4
Number of Residues17
Detailsbinding site for residue GDP B 501
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BSER138
BGLY141
BGLY142
BTHR143
BGLY144
BPRO171
BVAL175
BASP177
BGLU181
BASN204
BTYR222
BASN226
BMG502

site_idAC5
Number of Residues3
Detailsbinding site for residue MG B 502
ChainResidue
BGLN11
BASP177
BGDP501

site_idAC6
Number of Residues7
Detailsbinding site for residue MES B 503
ChainResidue
BARG156
BPRO160
BASP161
BARG162
BASN195
BASP197
BARG251

site_idAC7
Number of Residues1
Detailsbinding site for residue CA B 504
ChainResidue
BGLU111

site_idAC8
Number of Residues7
Detailsbinding site for residue MES B 505
ChainResidue
BPHE294
BASP295
BSER296
BPRO305
BARG306
BTYR310
BASN337

site_idAC9
Number of Residues16
Detailsbinding site for residue 9LX B 506
ChainResidue
ATHR179
AVAL181
BVAL236
BCYS239
BLEU246
BASP249
BLEU253
BASN256
BMET257
BVAL313
BALA314
BVAL316
BASN348
BLYS350
BTHR351
BALA352

site_idAD1
Number of Residues23
Detailsbinding site for residue GTP C 501
ChainResidue
CASN228
CILE231
CMG502
CHOH601
CHOH602
CHOH604
DLYS252
CGLN11
CALA12
CGLN15
CASP98
CALA99
CALA100
CASN101
CSER140
CGLY143
CGLY144
CTHR145
CGLY146
CVAL177
CGLU183
CASN206
CTYR224

site_idAD2
Number of Residues5
Detailsbinding site for residue MG C 502
ChainResidue
CGTP501
CHOH601
CHOH602
CHOH603
CHOH604

site_idAD3
Number of Residues4
Detailsbinding site for residue CA C 503
ChainResidue
CASP39
CTHR41
CGLY44
CGLU55

site_idAD4
Number of Residues18
Detailsbinding site for residue GTP D 501
ChainResidue
DGLY10
DGLN11
DCYS12
DALA97
DGLY98
DASN99
DSER138
DGLY141
DGLY142
DTHR143
DGLY144
DVAL175
DSER176
DGLU181
DASN204
DTYR222
DASN226
DMG502

site_idAD5
Number of Residues1
Detailsbinding site for residue MG D 502
ChainResidue
DGTP501

site_idAD6
Number of Residues15
Detailsbinding site for residue 9LX D 503
ChainResidue
CTHR179
CVAL181
DVAL236
DCYS239
DLEU240
DLEU246
DASP249
DLYS252
DLEU253
DASN256
DVAL313
DVAL316
DLYS350
DTHR351
DALA352

site_idAD7
Number of Residues16
Detailsbinding site for residue ACP F 401
ChainResidue
FLYS74
FLYS150
FGLN183
FLYS184
FLEU186
FLYS198
FASP200
FARG202
FARG222
FTHR241
FASN242
FASP318
FMET320
FILE330
FGLU331
FASN333

Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
AGLY142-GLY148
BGLY140-GLY146

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
BGLY142
BTHR143
BGLY144
BASN204
BASN226
DGLN11
DSER138
DGLY142
DTHR143
DGLY144
DASN204
DASN226
ESER46
BSER138

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
DGLU69
BGLU69

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
CSER48
CSER232
BTHR55
DTHR55

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
BLYS58
DLYS58

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1
ChainResidueDetails
BSER172
DSER172

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
DTHR285
DTHR290
BTHR285
BTHR290

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BARG318
DARG318

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q2T9S0
ChainResidueDetails
BGLU438
DGLU438

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
BLYS58
ALYS370
CLYS326
CLYS370
DLYS58

site_idSWS_FT_FI11
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BLYS324
DLYS324

218500

PDB entries from 2024-04-17

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