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5XKE

Crystal structure of T2R-TTL-Demecolcine 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
ATHR179
AGLU183
AASN206
ATYR224
AASN228
AILE231
AGLN11
AMG502
AHOH603
AHOH609
AHOH613
AHOH615
AHOH619
AHOH641
BLYS252
AALA12
AGLN15
AASP98
AALA99
AASN101
ASER140
AGLY143

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 502
ChainResidue
AGTP501
AHOH613
AHOH615
AHOH619
AHOH641

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

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 504
ChainResidue
AASN216
APRO274
AVAL275
AALA294
AHOH608
AHOH610
AHOH612

site_idAC5
Number of Residues25
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
BHOH601
BHOH602
BHOH607
BHOH609
BHOH620
BHOH622
BHOH624
BHOH637

site_idAC6
Number of Residues7
Detailsbinding site for residue MG B 502
ChainResidue
BGLN11
BGDP501
BHOH617
BHOH622
BHOH637
BHOH644
CHOH622

site_idAC7
Number of Residues9
Detailsbinding site for residue MES B 503
ChainResidue
BARG156
BPRO160
BASP161
BARG162
BILE163
BASN195
BTHR196
BASP197
BARG251

site_idAC8
Number of Residues12
Detailsbinding site for residue LON B 504
ChainResidue
AVAL181
BCYS239
BALA248
BLYS252
BLEU253
BASN256
BVAL313
BALA314
BILE316
BASN348
BLYS350
BILE368

site_idAC9
Number of Residues28
Detailsbinding site for residue GTP C 501
ChainResidue
CGLN15
CASP98
CALA99
CASN101
CSER140
CGLY143
CGLY144
CTHR145
CGLY146
CILE171
CVAL177
CTHR179
CGLU183
CASN206
CTYR224
CASN228
CILE231
CMG502
CHOH612
CHOH613
CHOH619
CHOH636
CHOH650
CHOH651
DLYS252
CGLY10
CGLN11
CALA12

site_idAD1
Number of Residues5
Detailsbinding site for residue MG C 502
ChainResidue
CGTP501
CHOH612
CHOH619
CHOH636
CHOH651

site_idAD2
Number of Residues5
Detailsbinding site for residue CA C 503
ChainResidue
CASP39
CTHR41
CGLY44
CASP47
CGLU55

site_idAD3
Number of Residues20
Detailsbinding site for residue GTP D 501
ChainResidue
DGLY10
DGLN11
DCYS12
DGLN15
DALA97
DGLY98
DASN99
DSER138
DGLY141
DGLY142
DTHR143
DGLY144
DVAL175
DSER176
DGLU181
DASN204
DTYR222
DASN226
DMG502
DHOH605

site_idAD4
Number of Residues3
Detailsbinding site for residue MG D 502
ChainResidue
DGLN11
DGLU69
DGTP501

site_idAD5
Number of Residues14
Detailsbinding site for residue LON D 503
ChainResidue
CTHR179
CVAL181
DVAL236
DCYS239
DLEU246
DALA248
DLYS252
DLEU253
DASN256
DVAL313
DALA314
DASN348
DLYS350
DILE368

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 Residues14
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q13509
ChainResidueDetails
DGLN11
DSER138
DGLY142
DTHR143
DGLY144
DASN204
DASN226
BGLN11
BSER138
BGLY142
BTHR143
BGLY144
BASN204
BASN226

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
BGLU69
DGLU69

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
BLYS58
DLYS58

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885
ChainResidueDetails
BSER172
DSER172
CSER48
CSER232

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
DTHR285
DTHR290
BTHR285
BTHR290

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BARG318
DARG318

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q2T9S0
ChainResidueDetails
BGLU438
DGLU438

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
BLYS58
DLYS58

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
DLYS324
BLYS324

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:Q71U36
ChainResidueDetails
CTYR451
ATYR451

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

221051

PDB entries from 2024-06-12

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