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7CE6

Crystal structure of T2R-TTL-Compound9 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 Residues23
Detailsbinding site for residue GTP A 501
ChainResidue
AGLY10
AGLY144
ATHR145
AGLY146
ASER178
AGLU183
AASN206
ATYR224
AASN228
AILE231
AMG502
AGLN11
AHOH623
AHOH634
AHOH649
BLYS252
AALA12
AGLN15
AASP98
AALA99
AASN101
ASER140
AGLY143

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 502
ChainResidue
AGTP501
AHOH611
AHOH623
AHOH649

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

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 504
ChainResidue
AASN216
APRO274
AVAL275
AILE276
AHOH653

site_idAC5
Number of Residues19
Detailsbinding site for residue GDP B 501
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BSER138
BGLY141
BGLY142
BTHR143
BGLY144
BVAL175
BASP177
BGLU181
BASN204
BTYR222
BASN226
BMG502
BHOH605
BHOH630
BHOH650

site_idAC6
Number of Residues6
Detailsbinding site for residue MG B 502
ChainResidue
BGLN11
BASP177
BGDP501
BHOH641
BHOH642
CHOH610

site_idAC7
Number of Residues8
Detailsbinding site for residue MES B 503
ChainResidue
BARG156
BASP161
BARG162
BILE163
BASN195
BTHR196
BASP197
BARG251

site_idAC8
Number of Residues15
Detailsbinding site for residue AF6 B 504
ChainResidue
BTYR50
BGLN134
BPHE167
BGLU198
BTYR200
BVAL236
BTHR237
BLEU240
BLEU246
BLEU250
BLEU253
BMET257
BALA314
BILE316
BHOH654

site_idAC9
Number of Residues25
Detailsbinding site for residue GTP C 501
ChainResidue
CASN206
CTYR224
CASN228
CILE231
CMG502
CHOH635
CHOH643
CHOH648
CHOH654
DLYS252
CGLY10
CGLN11
CALA12
CGLN15
CASP98
CALA99
CALA100
CASN101
CSER140
CGLY143
CGLY144
CTHR145
CGLY146
CVAL177
CGLU183

site_idAD1
Number of Residues4
Detailsbinding site for residue MG C 502
ChainResidue
CGTP501
CHOH643
CHOH648
CHOH654

site_idAD2
Number of Residues5
Detailsbinding site for residue CA C 503
ChainResidue
CASP39
CTHR41
CGLY44
CGLU55
CHOH608

site_idAD3
Number of Residues18
Detailsbinding site for residue GTP D 501
ChainResidue
DGLY10
DGLN11
DCYS12
DGLN15
DALA97
DASN99
DSER138
DGLY141
DGLY142
DTHR143
DGLY144
DVAL175
DSER176
DGLU181
DASN204
DTYR222
DASN226
DMG503

site_idAD4
Number of Residues15
Detailsbinding site for residue AF6 D 502
ChainResidue
DTYR50
DGLN134
DASN165
DPHE167
DGLU198
DTYR200
DVAL236
DTHR237
DCYS239
DLEU240
DLEU250
DLEU253
DMET257
DALA314
DALA352

site_idAD5
Number of Residues3
Detailsbinding site for residue MG D 503
ChainResidue
DASP67
DGLU69
DGTP501

site_idAD6
Number of Residues15
Detailsbinding site for residue ACP F 401
ChainResidue
FLYS74
FLYS184
FTYR185
FLEU186
FLYS198
FASP200
FARG202
FARG222
FLEU240
FTHR241
FASN242
FASP318
FMET320
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 Residues14
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q13509
ChainResidueDetails
BGLN11
DGLY142
DTHR143
DGLY144
DASN204
DASN226
BSER138
BGLY142
BTHR143
BGLY144
BASN204
BASN226
DGLN11
DSER138

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
BGLU69
CGLU71
CSER140
CGLY144
CTHR145
CTHR179
CASN206
CASN228
DGLU69
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
BLYS58
DLYS58
CSER48
CSER232

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

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

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
ALYS326
BLYS324
ALYS370
DLYS324
CLYS370

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PDB entries from 2024-07-24

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