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

6WWL

KIF14[391-755] dimer two-heads-bound state - AMP-PNP in complex with 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
B0003924molecular_functionGTPase activity
B0005200molecular_functionstructural constituent of cytoskeleton
B0005525molecular_functionGTP binding
B0005874cellular_componentmicrotubule
B0007017biological_processmicrotubule-based process
E0000226biological_processmicrotubule cytoskeleton organization
E0000278biological_processmitotic cell cycle
E0003924molecular_functionGTPase activity
E0005200molecular_functionstructural constituent of cytoskeleton
E0005525molecular_functionGTP binding
E0005737cellular_componentcytoplasm
E0005856cellular_componentcytoskeleton
E0005874cellular_componentmicrotubule
E0007017biological_processmicrotubule-based process
E0015630cellular_componentmicrotubule cytoskeleton
E0016787molecular_functionhydrolase activity
E0046872molecular_functionmetal ion binding
I0003924molecular_functionGTPase activity
I0005200molecular_functionstructural constituent of cytoskeleton
I0005525molecular_functionGTP binding
I0005874cellular_componentmicrotubule
I0007017biological_processmicrotubule-based process
K0003777molecular_functionmicrotubule motor activity
K0005524molecular_functionATP binding
K0007018biological_processmicrotubule-based movement
K0008017molecular_functionmicrotubule binding
N0003777molecular_functionmicrotubule motor activity
N0005524molecular_functionATP binding
N0007018biological_processmicrotubule-based movement
N0008017molecular_functionmicrotubule binding
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_idPS00411
Number of Residues12
DetailsKINESIN_MOTOR_1 Kinesin motor domain signature. SRInLVDLAGSE
ChainResidueDetails
KSER632-GLU643

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00283, ECO:0007744|PDB:4OZQ
ChainResidueDetails
KGLY482
NGLY482

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
AGLN11
EGLU71
ESER140
EGLY144
ETHR145
ETHR179
EASN206
EASN228
AGLU71
ASER140
AGLY144
ATHR145
ATHR179
AASN206
AASN228
EGLN11

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Involved in polymerization => ECO:0000250
ChainResidueDetails
ATYR451
ETYR451

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
ALYS40
ELYS40

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
ASER48
ASER232
ESER48
ESER232

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P68373
ChainResidueDetails
ATYR282
ETYR282

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
AARG339
EARG339

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68373
ChainResidueDetails
ASER439
ESER439

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
AGLU443
EGLU443

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:P68369
ChainResidueDetails
AGLU445
EGLU445

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:Q71U36
ChainResidueDetails
ATYR451
ETYR451

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
ELYS326
ELYS370

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon