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6O5N

Tubulin-RB3_SLD-TTL in complex with compound 10ab

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 Residues20
Detailsbinding site for residue GTP A 501
ChainResidue
AGLY10
AGLY144
ATHR145
AGLY146
AVAL177
ATHR179
AGLU183
AASN206
ATYR224
AASN228
AILE231
AGLN11
AMG502
AALA12
AGLN15
AASP98
AALA99
AASN101
ASER140
AGLY143

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 502
ChainResidue
AASP69
AGLU71
AGTP501

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
BVAL175
BASP177
BGLU181
BASN204
BTYR222
BASN226
BMG502
BHOH603

site_idAC5
Number of Residues4
Detailsbinding site for residue MG B 502
ChainResidue
BGLN11
BASP177
BGDP501
BHOH603

site_idAC6
Number of Residues6
Detailsbinding site for residue MES B 503
ChainResidue
BARG156
BASP161
BARG162
BASN195
BASP197
BARG251

site_idAC7
Number of Residues6
Detailsbinding site for residue MES B 504
ChainResidue
BPHE294
BASP295
BSER296
BARG306
BASN337
BTYR340

site_idAC8
Number of Residues14
Detailsbinding site for residue QW9 B 505
ChainResidue
ATHR179
AALA180
AVAL181
BVAL236
BCYS239
BLEU240
BALA248
BASP249
BASN256
BVAL313
BALA314
BASN348
BLYS350
BHOH602

site_idAC9
Number of Residues21
Detailsbinding site for residue GTP C 501
ChainResidue
CGLY10
CGLN11
CALA12
CGLN15
CASP98
CALA99
CALA100
CASN101
CSER140
CGLY143
CGLY144
CTHR145
CGLY146
CVAL177
CTHR179
CGLU183
CASN206
CTYR224
CASN228
CILE231
CMG502

site_idAD1
Number of Residues3
Detailsbinding site for residue MG C 502
ChainResidue
CASP69
CGLU71
CGTP501

site_idAD2
Number of Residues4
Detailsbinding site for residue CA C 503
ChainResidue
CTHR41
CGLY44
CGLU55
CASP39

site_idAD3
Number of Residues13
Detailsbinding site for residue GDP D 501
ChainResidue
DGLY10
DGLN11
DCYS12
DGLN15
DSER138
DGLY141
DTHR143
DGLY144
DSER176
DGLU181
DASN204
DTYR222
DASN226

site_idAD4
Number of Residues16
Detailsbinding site for residue QW9 D 502
ChainResidue
CTHR179
CALA180
DVAL236
DCYS239
DLEU240
DALA248
DASP249
DLYS252
DASN256
DMET257
DVAL313
DILE316
DASN348
DLYS350
DALA352
DHOH601

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
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

222036

PDB entries from 2024-07-03

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