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6KPP

BNC105 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
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 Residues21
Detailsbinding site for residue GTP A 501
ChainResidue
AGLY10
AGLY144
ATHR145
AGLY146
AILE171
AVAL177
ASER178
AGLU183
AASN206
ATYR224
AASN228
AGLN11
AILE231
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 Residues15
Detailsbinding site for residue DO6 B 501
ChainResidue
ATHR179
AALA180
AVAL181
BVAL236
BCYS239
BLEU240
BALA248
BASP249
BLYS252
BLEU253
BASN256
BVAL313
BILE316
BASN348
BLYS350

site_idAC5
Number of Residues5
Detailsbinding site for residue MG B 502
ChainResidue
BGLN11
BASP177
BGDP503
BHOH624
CHOH622

site_idAC6
Number of Residues18
Detailsbinding site for residue GDP B 503
ChainResidue
BGLY10
BGLN11
BCYS12
BGLN15
BSER138
BGLY141
BGLY142
BTHR143
BGLY144
BVAL175
BASP177
BGLU181
BASN204
BTYR222
BASN226
BMG502
BHOH612
BHOH615

site_idAC7
Number of Residues6
Detailsbinding site for residue MES B 504
ChainResidue
BARG156
BASP161
BARG162
BASN195
BASP197
BARG251

site_idAC8
Number of Residues7
Detailsbinding site for residue MES B 505
ChainResidue
BPHE294
BASP295
BSER296
BASP304
BARG306
BASN337
BTYR340

site_idAC9
Number of Residues3
Detailsbinding site for residue GOL B 506
ChainResidue
BVAL175
BPRO220
BTYR222

site_idAD1
Number of Residues20
Detailsbinding site for residue GTP C 501
ChainResidue
CTYR224
CASN228
CMG502
CGLY10
CGLN11
CALA12
CGLN15
CASP98
CALA99
CASN101
CSER140
CGLY142
CGLY143
CGLY144
CTHR145
CGLY146
CVAL177
CTHR179
CGLU183
CASN206

site_idAD2
Number of Residues2
Detailsbinding site for residue MG C 502
ChainResidue
CGLU71
CGTP501

site_idAD3
Number of Residues4
Detailsbinding site for residue CA C 503
ChainResidue
CASP39
CTHR41
CGLY44
CGLU55

site_idAD4
Number of Residues3
Detailsbinding site for residue GOL C 504
ChainResidue
CVAL177
CPRO222
DGLN245

site_idAD5
Number of Residues16
Detailsbinding site for residue DO6 D 501
ChainResidue
CTHR179
CALA180
CVAL181
DVAL236
DCYS239
DLEU246
DALA248
DLYS252
DLEU253
DASN256
DMET257
DVAL313
DILE316
DASN348
DLYS350
DILE368

site_idAD6
Number of Residues4
Detailsbinding site for residue MG D 502
ChainResidue
DGLN11
DASN99
DASP177
DGDP503

site_idAD7
Number of Residues17
Detailsbinding site for residue GDP D 503
ChainResidue
DGLY10
DGLN11
DCYS12
DGLN15
DILE16
DSER138
DGLY141
DGLY142
DTHR143
DGLY144
DVAL175
DASP177
DGLU181
DASN204
DTYR222
DASN226
DMG502

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
EPRO38-GLU47

site_idPS01041
Number of Residues10
DetailsSTATHMIN_2 Stathmin family signature 2. AEKREHEREV
ChainResidueDetails
EALA71-VAL80

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q13509
ChainResidueDetails
BGLY142
BTHR143
BGLY144
BASN204
BASN226
DGLN11
DSER138
DGLY142
DTHR143
DGLY144
DASN204
DASN226
BSER138
BGLN11

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
CSER48
CSER232
BLYS58
DLYS58

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
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
DLYS58
BLYS58

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
ALYS370
DLYS324
CLYS370
BLYS324

219869

PDB entries from 2024-05-15

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