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5GON

Structures of a beta-lactam bridged analogue in complex with tubulin

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
A0005829cellular_componentcytosol
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
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
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
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 Residues23
Detailsbinding site for residue GTP A 501
ChainResidue
AGLY10
AGLY144
ATHR145
AGLY146
AVAL177
ATHR179
AGLU183
AASN206
ATYR224
AASN228
AILE231
AGLN11
AMG502
AHOH611
AHOH612
AHOH635
AALA12
AGLN15
AASP98
AALA99
AASN101
ASER140
AGLY143

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 502
ChainResidue
AGTP501
AHOH611
AHOH635

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 503
ChainResidue
AASN216
APRO274
AVAL275
AALA294
AASN300

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 504
ChainResidue
AHIS309
AGLY310
ATHR382
AALA383
AALA385
AGLU386
FARG66

site_idAC5
Number of Residues4
Detailsbinding site for residue CA A 505
ChainResidue
AASP39
ATHR41
AGLY44
AGLU55

site_idAC6
Number of Residues4
Detailsbinding site for residue GOL A 506
ChainResidue
ALYS164
ALYS166
AGLU196
EASP44

site_idAC7
Number of Residues21
Detailsbinding site for residue GDP B 501
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BSER140
BGLY143
BGLY144
BTHR145
BGLY146
BVAL177
BASP179
BGLU183
BASN206
BTYR224
BASN228
BMG502
BHOH603
BHOH604
BHOH613
BHOH625
BHOH631

site_idAC8
Number of Residues4
Detailsbinding site for residue MG B 502
ChainResidue
BGLN11
BASP179
BGDP501
BHOH648

site_idAC9
Number of Residues4
Detailsbinding site for residue GOL B 503
ChainResidue
BARG401
CTYR262
CGLU434
CVAL435

site_idAD1
Number of Residues2
Detailsbinding site for residue GOL B 504
ChainResidue
BVAL177
BPRO222

site_idAD2
Number of Residues10
Detailsbinding site for residue GOL B 505
ChainResidue
BGLU27
BALA233
BSER236
BGLY237
BPHE272
BARG320
BPRO360
BSER374
BALA375
BTHR376

site_idAD3
Number of Residues1
Detailsbinding site for residue CA B 506
ChainResidue
BGLU113

site_idAD4
Number of Residues8
Detailsbinding site for residue MES B 507
ChainResidue
BARG158
BPRO162
BASP163
BARG164
BILE165
BASN197
BASP199
BARG253

site_idAD5
Number of Residues14
Detailsbinding site for residue 6ZR B 508
ChainResidue
BGLY237
BVAL238
BCYS241
BALA250
BASP251
BLYS254
BLEU255
BASN258
BALA317
BILE318
BLYS352
ATHR179
AALA180
AVAL181

site_idAD6
Number of Residues3
Detailsbinding site for residue GOL C 502
ChainResidue
BLYS105
CTHR253
CTHR257

site_idAD7
Number of Residues23
Detailsbinding site for residue GTP C 503
ChainResidue
CGLY10
CGLN11
CALA12
CGLN15
CASP98
CALA99
CALA100
CASN101
CSER140
CGLY143
CGLY144
CTHR145
CGLY146
CVAL177
CTHR179
CGLU183
CASN206
CTYR224
CASN228
CMG504
CHOH621
CHOH628
DLYS254

site_idAD8
Number of Residues2
Detailsbinding site for residue MG C 504
ChainResidue
CGTP503
CHOH628

site_idAD9
Number of Residues6
Detailsbinding site for residue GOL C 505
ChainResidue
CVAL177
CARG221
CPRO222
CTHR223
CTYR224
DGLN247

site_idAE1
Number of Residues6
Detailsbinding site for residue GOL C 506
ChainResidue
CSER287
CVAL288
CASP322
CASP327
CARG373
CHOH601

site_idAE2
Number of Residues6
Detailsbinding site for residue GOL C 507
ChainResidue
CLYS163
CLYS164
CLYS166
CGLU196
CHIS197
CASP199

site_idAE3
Number of Residues3
Detailsbinding site for residue IMD C 508
ChainResidue
CASP431
CHOH626
CHOH672

site_idAE4
Number of Residues5
Detailsbinding site for residue IMD C 509
ChainResidue
CGLY410
CGLU411
DGOL504
EARG112
ELEU116

site_idAE5
Number of Residues3
Detailsbinding site for residue IMD C 510
ChainResidue
CSER165
CLEU167
CGLN256

site_idAE6
Number of Residues17
Detailsbinding site for residue GDP D 501
ChainResidue
DGLY10
DGLN11
DCYS12
DGLN15
DSER140
DGLY142
DGLY143
DGLY144
DTHR145
DGLY146
DASP179
DGLU183
DASN206
DTYR224
DASN228
DMG502
DHOH603

site_idAE7
Number of Residues3
Detailsbinding site for residue MG D 502
ChainResidue
DGLN11
DASP179
DGDP501

site_idAE8
Number of Residues3
Detailsbinding site for residue GOL D 503
ChainResidue
DVAL177
DPRO222
DTYR224

site_idAE9
Number of Residues7
Detailsbinding site for residue GOL D 504
ChainResidue
CIMD509
DARG158
DPRO162
DASP163
DARG164
DASP199
DARG253

site_idAF1
Number of Residues1
Detailsbinding site for residue MG F 401
ChainResidue
FGLU331

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

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
BGLU71
CGLU71
CSER140
CGLY144
CTHR145
CTHR179
CASN206
CASN228
DGLU71
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: Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8
ChainResidueDetails
BTHR57
DTHR57
CSER48
CSER232

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

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

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

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BARG320
DARG320
ALYS370
CLYS326
CLYS370

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
BLYS60
DLYS60

site_idSWS_FT_FI10
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BLYS326
DLYS326

225681

PDB entries from 2024-10-02

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