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7LVQ

KIF14[391-743] - AMP-PNP closed state class 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
K0003777molecular_functionmicrotubule motor activity
K0005524molecular_functionATP binding
K0007018biological_processmicrotubule-based movement
K0008017molecular_functionmicrotubule binding
Functional Information from PROSITE/UniProt
site_idPS00411
Number of Residues12
DetailsKINESIN_MOTOR_1 Kinesin motor domain signature. SRInLVDLAGSE
ChainResidueDetails
KSER632-GLU643

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00283, ECO:0007744|PDB:4OZQ
ChainResidueDetails
KGLY482

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
AGLN11
AGLU71
ASER140
AGLY144
ATHR145
ATHR179
AASN206
AASN228

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Involved in polymerization => ECO:0000250
ChainResidueDetails
ATYR451

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
ALYS40

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
ASER48
ASER232

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P68373
ChainResidueDetails
ATYR282

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
AARG339

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68373
ChainResidueDetails
ASER439

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
AGLU443

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:P68369
ChainResidueDetails
AGLU445

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:Q71U36
ChainResidueDetails
ATYR451

site_idSWS_FT_FI12
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
ALYS326
ALYS370

219140

PDB entries from 2024-05-01

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