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7X4N

Crystal Structure of C. elegans kinesin-4 KLP-12 complexed with tubulin and DARPin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0005200molecular_functionstructural constituent of cytoskeleton
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0007017biological_processmicrotubule-based process
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
E0003777molecular_functionmicrotubule motor activity
E0005524molecular_functionATP binding
E0007018biological_processmicrotubule-based movement
E0008017molecular_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. AKFhFVDLAGSE
ChainResidueDetails
EALA255-GLU266

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00283, ECO:0000305|PubMed:36065637, ECO:0000312|PDB:7X4N
ChainResidueDetails
EGLY84
BSER138
BGLY142
BTHR143
BGLY144
BASN204
BASN226

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:36065637, ECO:0000312|PDB:7X4N
ChainResidueDetails
ETHR91
ESER217
ASER140
AGLY144
ATHR145
ATHR179
AASN206
AASN228

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
BSER40

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
BLYS58

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885
ChainResidueDetails
BSER172

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BTHR285
BTHR290

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BARG318

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q2T9S0
ChainResidueDetails
BGLU438

site_idSWS_FT_FI9
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BLYS58

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BLYS324

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PDB entries from 2024-07-10

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