Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6B0C

KLP10A-AMPPNP in complex with curved tubulin and a microtubule

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
K0003777molecular_functionmicrotubule motor activity
K0005524molecular_functionATP binding
K0007018biological_processmicrotubule-based movement
K0008017molecular_functionmicrotubule binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue GTP A 501
ChainResidue
AGLN11
AGLY144
ATHR145
APRO173
ATHR179
AASN206
ATYR224
AASN228
AMG502
BLYS252
AALA12
AGLN15
AGLU71
AALA99
AALA100
AASN101
ASER140
AGLY143

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 502
ChainResidue
AGLU71
AGTP501
BLYS252

site_idAC3
Number of Residues15
Detailsbinding site for residue GDP B 501
ChainResidue
BGLN11
BCYS12
BGLN15
BGLU69
BALA97
BASN99
BSER138
BGLY141
BGLY142
BTHR143
BGLY144
BGLU181
BASN204
BTYR222
BASN226

site_idAC4
Number of Residues22
Detailsbinding site for residue GTP C 501
ChainResidue
CGLY10
CGLN11
CALA12
CGLN15
CASP98
CALA99
CALA100
CASN101
CSER140
CGLY142
CGLY143
CGLY144
CTHR145
CGLY146
CILE171
CTHR179
CASN206
CTYR224
CASN228
CMG502
DLEU246
DLYS252

site_idAC5
Number of Residues2
Detailsbinding site for residue MG C 502
ChainResidue
CGLU71
CGTP501

site_idAC6
Number of Residues14
Detailsbinding site for residue GDP D 501
ChainResidue
DGLY10
DGLN11
DCYS12
DGLN15
DASN99
DSER138
DGLY141
DGLY142
DTHR143
DGLY144
DASP177
DASN204
DTYR222
DASN226

site_idAC7
Number of Residues13
Detailsbinding site for residue TA1 D 502
ChainResidue
DVAL23
DGLU27
DLEU215
DASP224
DHIS227
DALA231
DPRO272
DLEU273
DTHR274
DARG276
DPRO358
DARG359
DLEU361

site_idAC8
Number of Residues3
Detailsbinding site for residue MG K 701
ChainResidue
KTHR375
KSER488
KANP702

site_idAC9
Number of Residues15
Detailsbinding site for residue ANP K 702
ChainResidue
KHIS376
KPHE382
KSER487
KSER488
KALA516
KMG701
KARG284
KPRO287
KGLN369
KTHR370
KGLY371
KSER372
KGLY373
KLYS374
KTHR375

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_idPS00411
Number of Residues12
DetailsKINESIN_MOTOR_1 Kinesin motor domain signature. GKFsFIDLAGNE
ChainResidueDetails
KGLY508-GLU519

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

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885
ChainResidueDetails
BSER172
DSER172
CSER48
CSER232

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
AGLU445
BLYS324
DLYS324

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:Q71U36
ChainResidueDetails
ATYR451
CTYR451

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

224931

PDB entries from 2024-09-11

PDB statisticsPDBj update infoContact PDBjnumon