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4ATX

Rigor kinesin motor domain with an ordered neck-linker, docked on tubulin dimer, modelled into the 8A cryo-EM map of doublecortin- microtubules decorated with kinesin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0001764biological_processneuron migration
A0003924molecular_functionGTPase activity
A0005200molecular_functionstructural constituent of cytoskeleton
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0007017biological_processmicrotubule-based process
A0007399biological_processnervous system development
A0015630cellular_componentmicrotubule cytoskeleton
A0046872molecular_functionmetal ion binding
A0046982molecular_functionprotein heterodimerization activity
A1902669biological_processpositive regulation of axon guidance
B0000166molecular_functionnucleotide binding
B0000226biological_processmicrotubule cytoskeleton organization
B0000278biological_processmitotic cell cycle
B0005200molecular_functionstructural constituent of cytoskeleton
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0007017biological_processmicrotubule-based process
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
C0003777molecular_functionmicrotubule motor activity
C0005524molecular_functionATP binding
C0007018biological_processmicrotubule-based movement
C0008017molecular_functionmicrotubule binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GDP A 600
ChainResidue
AGLY10
AASP179
AASN206
ATYR224
AASN228
AGLN11
ACYS12
AGLN15
ASER140
AGLY142
AGLY144
ATHR145
AGLY146

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GTP B 500
ChainResidue
ALEU248
ALYS254
BGLY10
BGLN11
BALA12
BGLN15
BALA99
BALA100
BASN101
BSER140
BGLY143
BGLY144
BTHR145
BGLY146
BILE171
BGLU183
BASN206
BTYR224
BASN228

Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
AGLY142-GLY148
BGLY142-GLY148

site_idPS00228
Number of Residues4
DetailsTUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI
ChainResidueDetails
AMET1-ILE4

site_idPS00411
Number of Residues12
DetailsKINESIN_MOTOR_1 Kinesin motor domain signature. GKLyLVDLAGSE
ChainResidueDetails
CGLY225-GLU236

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q3KRE8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"UniProtKB","id":"Q9BVA1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00283","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P33176","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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