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4O4L

Tubulin-Peloruside A-Epothilone A 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
A0005829cellular_componentcytosol
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
C0005829cellular_componentcytosol
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 Residues26
DetailsBINDING SITE FOR RESIDUE GTP A 501
ChainResidue
AGLY10
AGLY143
AGLY144
ATHR145
AGLY146
AVAL177
AGLU183
AASN206
ATYR224
AASN228
AILE231
AGLN11
AMG502
AHOH601
AHOH602
AHOH605
AHOH613
AHOH657
BLYS254
AALA12
AGLN15
AASP98
AALA99
AALA100
AASN101
ASER140

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AGTP501
AHOH601
AHOH605
AHOH613
AHOH648

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 503
ChainResidue
AASP39
ATHR41
AGLY44
AGLU55
AHOH714

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GDP B 501
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BSER140
BGLY143
BGLY144
BTHR145
BGLY146
BVAL177
BASP179
BGLU183
BASN206
BTYR224
BASN228
BMG502
BHOH601
BHOH603
BHOH605
BHOH618
BHOH633
BHOH702

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 502
ChainResidue
BGLN11
BGDP501
BHOH630
BHOH632
BHOH702
CHOH637

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE POU B 503
ChainResidue
BGLN293
BPHE296
BASP297
BSER298
BARG308
BTYR312
BASN339
BTYR342

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE EP B 504
ChainResidue
BLEU217
BLEU219
BASP226
BHIS229
BPHE272
BPRO274
BLEU275
BTHR276
BGLN281
BGLN282
BLEU371

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA B 505
ChainResidue
BHOH656

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA B 506
ChainResidue
BGLU113
CHOH603

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MES B 507
ChainResidue
BARG158
BPRO162
BASP163
BARG164
BASN197
BASP199
BARG253

site_idBC2
Number of Residues28
DetailsBINDING SITE FOR RESIDUE GTP C 501
ChainResidue
CALA100
CASN101
CSER140
CGLY143
CGLY144
CTHR145
CGLY146
CILE171
CVAL177
CTHR179
CGLU183
CASN206
CTYR224
CASN228
CILE231
CMG502
CHOH601
CHOH609
CHOH610
CHOH613
CHOH699
DLYS254
CGLY10
CGLN11
CALA12
CGLN15
CASP98
CALA99

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG C 502
ChainResidue
CGTP501
CHOH601
CHOH604
CHOH610

site_idBC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP D 501
ChainResidue
DGLY10
DGLN11
DCYS12
DGLN15
DSER140
DGLY143
DGLY144
DTHR145
DGLY146
DSER178
DGLU183
DASN206
DTYR224
DASN228
DMG502
DHOH608
DHOH609
DHOH610
DHOH611
DHOH624
DHOH625

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 502
ChainResidue
DGLN11
DGDP501
DHOH604
DHOH608
DHOH609
DHOH638

site_idBC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE POU D 503
ChainResidue
DGLN293
DPHE296
DASP297
DSER298
DPRO307
DARG308
DTYR312
DVAL335
DASN339
DTYR342

site_idBC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EP D 504
ChainResidue
DLEU217
DASP226
DHIS229
DPHE272
DPRO274
DLEU275
DTHR276
DARG284
DLEU371

Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
AGLY142-GLY148
BGLY142-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
BGLY144
BTHR145
BGLY146
BASN206
BASN228
DGLN11
DSER140
DGLY144
DTHR145
DGLY146
DASN206
DASN228
ESER46
BSER140

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
DGLU71
BGLU71

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
BTHR57
DTHR57

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
DLYS60
CSER48
CSER232
BLYS60

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1
ChainResidueDetails
DSER174
BSER174

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
DTHR287
DTHR292
BTHR287
BTHR292

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BARG320
DARG320

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q2T9S0
ChainResidueDetails
BGLU448
DGLU448

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
BLYS60
DLYS60

site_idSWS_FT_FI11
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BLYS326
ATYR451
DLYS326

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

218500

PDB entries from 2024-04-17

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