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5CA0

Crystal structure of T2R-TTL-Lexibulin 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
B0003924molecular_functionGTPase activity
B0005200molecular_functionstructural constituent of cytoskeleton
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0007010biological_processcytoskeleton organization
B0007017biological_processmicrotubule-based process
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
D0003924molecular_functionGTPase activity
D0005200molecular_functionstructural constituent of cytoskeleton
D0005525molecular_functionGTP binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005874cellular_componentmicrotubule
D0007010biological_processcytoskeleton organization
D0007017biological_processmicrotubule-based process
E0031110biological_processregulation of microtubule polymerization or depolymerization
F0036211biological_processprotein modification process
Functional Information from PDB Data
site_idAC1
Number of Residues24
Detailsbinding site for residue GTP A 501
ChainResidue
AGLY10
AGLY143
AGLY144
ATHR145
AGLY146
ASER178
AGLU183
AASN206
ATYR224
AASN228
AILE231
AGLN11
AMG502
AHOH606
AHOH607
AHOH630
BLYS252
AALA12
AGLN15
AASP98
AALA99
AALA100
AASN101
ASER140

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 502
ChainResidue
AGLU71
AGTP501
AHOH606
AHOH607
AHOH608
AHOH630

site_idAC3
Number of Residues5
Detailsbinding site for residue CA A 503
ChainResidue
AASP39
ATHR41
AGLY44
AGLU55
AHOH604

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 504
ChainResidue
AASN216
AVAL275
AALA294
AASN300

site_idAC5
Number of Residues19
Detailsbinding site for residue GDP B 501
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BASN99
BSER138
BGLY141
BGLY142
BTHR143
BGLY144
BVAL175
BASP177
BGLU181
BASN204
BTYR222
BASN226
BMG502
BHOH601
BHOH618

site_idAC6
Number of Residues5
Detailsbinding site for residue MG B 502
ChainResidue
BGLN11
BASP177
BGDP501
BHOH618
CHOH609

site_idAC7
Number of Residues9
Detailsbinding site for residue MES B 503
ChainResidue
BARG156
BPRO160
BASP161
BARG162
BGLU194
BASN195
BTHR196
BASP197
BARG251

site_idAC8
Number of Residues17
Detailsbinding site for residue LXL B 504
ChainResidue
ATHR179
BASN165
BGLU198
BTYR200
BVAL236
BTHR237
BLEU240
BALA248
BASP249
BLEU250
BLYS252
BLEU253
BVAL313
BALA314
BILE316
BLYS350
BALA352

site_idAC9
Number of Residues24
Detailsbinding site for residue GTP C 501
ChainResidue
CGLY144
CTHR145
CGLY146
CILE171
CGLU183
CASN206
CTYR224
CASN228
CILE231
CMG502
CHOH612
CHOH617
CHOH628
DLYS252
CGLY10
CGLN11
CALA12
CGLN15
CASP98
CALA99
CALA100
CASN101
CSER140
CGLY143

site_idAD1
Number of Residues5
Detailsbinding site for residue MG C 502
ChainResidue
CGTP501
CHOH607
CHOH612
CHOH617
CHOH628

site_idAD2
Number of Residues5
Detailsbinding site for residue CA C 503
ChainResidue
CASP39
CTHR41
CGLY44
CGLU55
CHOH601

site_idAD3
Number of Residues13
Detailsbinding site for residue GDP D 501
ChainResidue
DGLY10
DGLN11
DCYS12
DGLN15
DSER138
DGLY141
DGLY142
DTHR143
DSER176
DGLU181
DASN204
DTYR222
DASN226

site_idAD4
Number of Residues21
Detailsbinding site for residue LXL D 502
ChainResidue
CTHR179
DASN165
DGLU198
DTYR200
DVAL236
DTHR237
DCYS239
DLEU240
DLEU246
DALA248
DASP249
DLEU250
DLYS252
DLEU253
DVAL313
DALA314
DILE316
DLYS350
DTHR351
DALA352
DHOH601

site_idAD5
Number of Residues14
Detailsbinding site for residue ACP F 401
ChainResidue
FLYS74
FGLN183
FLYS184
FTYR185
FLEU186
FLYS198
FARG202
FARG222
FLEU240
FTHR241
FASN242
FASP318
FGLU331
FASN333

Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
BGLY140-GLY146
AGLY142-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
CGLU254

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
AGLN11
CGLU71
CSER140
CGLY144
CTHR145
CTHR179
CASN206
CASN228
AGLU71
ASER140
AGLY144
ATHR145
ATHR179
AASN206
AASN228
CGLN11

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Involved in polymerization => ECO:0000250
ChainResidueDetails
ATYR451
CTYR451

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
ALYS40
CLYS40

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
ASER48
ASER232
CSER48
CSER232

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P68373
ChainResidueDetails
ATYR282
CTYR282

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
AARG339
CARG339

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68373
ChainResidueDetails
ASER439
CSER439

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
AGLU443
CGLU443

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:P68369
ChainResidueDetails
AGLU445
CGLU445

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

219869

PDB entries from 2024-05-15

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