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4UXR

Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins

Functional Information from GO Data
ChainGOidnamespacecontents
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0003725molecular_functiondouble-stranded RNA binding
A0003924molecular_functionGTPase activity
A0005200molecular_functionstructural constituent of cytoskeleton
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0005881cellular_componentcytoplasmic microtubule
A0007017biological_processmicrotubule-based process
A0015630cellular_componentmicrotubule cytoskeleton
A0016787molecular_functionhydrolase activity
A0031625molecular_functionubiquitin protein ligase binding
A0046872molecular_functionmetal ion binding
A0071353biological_processcellular response to interleukin-4
B0000226biological_processmicrotubule cytoskeleton organization
B0000278biological_processmitotic cell cycle
B0003924molecular_functionGTPase activity
B0005200molecular_functionstructural constituent of cytoskeleton
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0007017biological_processmicrotubule-based process
B0007399biological_processnervous system development
B0015630cellular_componentmicrotubule cytoskeleton
B0046872molecular_functionmetal ion binding
B0046982molecular_functionprotein heterodimerization activity
B1902669biological_processpositive regulation of axon guidance
C0003777molecular_functionmicrotubule motor activity
C0005524molecular_functionATP binding
C0007018biological_processmicrotubule-based movement
C0008017molecular_functionmicrotubule binding
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AHIS256

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AGTP1413

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GTP A 1413
ChainResidue
ATHR118
AMG502
AGLY9
AGLN10
AALA11
AALA72
AASN74
AGLY116
AGLY117

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GDP B 1427
ChainResidue
BGLY9
BCYS11
BTHR142
BGLY143

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE TA1 B 1428
ChainResidue
BVAL22
BLEU272
BARG275
BPRO357
BARG358

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ADP C 1361
ChainResidue
CGLY102
CSER104
CMG1362
CALF1363

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG C 1362
ChainResidue
CADP1361
CALF1363

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ALF C 1363
ChainResidue
CSER214
CALA250
CGLY251
CADP1361
CMG1362

Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
BGLY139-GLY145
AGLY115-GLY121

site_idPS00228
Number of Residues4
DetailsTUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI
ChainResidueDetails
BMET0-ILE3

site_idPS00411
Number of Residues12
DetailsKINESIN_MOTOR_1 Kinesin motor domain signature. SKIsLVDLAGSE
ChainResidueDetails
CSER242-GLU253

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00283
ChainResidueDetails
CGLY97
BSER137
BGLY141
BTHR142
BGLY143
BASN203
BASN225

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
BGLU68
AGLU44
ASER113
AGLY117
ATHR118
ATHR152
AASN179
AASN201

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
BSER39

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8
ChainResidueDetails
BALA54

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024
ChainResidueDetails
BLYS57
AGLY205

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1
ChainResidueDetails
BSER171

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BTHR284
BTHR289

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BARG317

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q2T9S0
ChainResidueDetails
BGLU437

site_idSWS_FT_FI10
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
BLYS57

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437
ChainResidueDetails
ATYR424
BLYS323

site_idSWS_FT_FI12
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363
ChainResidueDetails
ALYS299
ALYS343

227111

PDB entries from 2024-11-06

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