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5EUQ

Crystal structure of an engineered construct of phosphatidylinositol 4 kinase III beta with a potent and selective inhibitor in complex with GDP loaded Rab11

Functional Information from GO Data
ChainGOidnamespacecontents
B0000139cellular_componentGolgi membrane
B0000166molecular_functionnucleotide binding
B0000922cellular_componentspindle pole
B0003924molecular_functionGTPase activity
B0003925molecular_functionG protein activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005768cellular_componentendosome
B0005771cellular_componentmultivesicular body
B0005794cellular_componentGolgi apparatus
B0005802cellular_componenttrans-Golgi network
B0005813cellular_componentcentrosome
B0005814cellular_componentcentriole
B0005828cellular_componentkinetochore microtubule
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006887biological_processexocytosis
B0007049biological_processcell cycle
B0007080biological_processmitotic metaphase chromosome alignment
B0008017molecular_functionmicrotubule binding
B0010008cellular_componentendosome membrane
B0010634biological_processpositive regulation of epithelial cell migration
B0010796biological_processregulation of multivesicular body size
B0010971biological_processpositive regulation of G2/M transition of mitotic cell cycle
B0015031biological_processprotein transport
B0016020cellular_componentmembrane
B0016192biological_processvesicle-mediated transport
B0016787molecular_functionhydrolase activity
B0019905molecular_functionsyntaxin binding
B0030133cellular_componenttransport vesicle
B0030659cellular_componentcytoplasmic vesicle membrane
B0030666cellular_componentendocytic vesicle membrane
B0030953biological_processastral microtubule organization
B0031175biological_processneuron projection development
B0031410cellular_componentcytoplasmic vesicle
B0031489molecular_functionmyosin V binding
B0031982cellular_componentvesicle
B0032154cellular_componentcleavage furrow
B0032402biological_processmelanosome transport
B0032465biological_processregulation of cytokinesis
B0032588cellular_componenttrans-Golgi network membrane
B0032991cellular_componentprotein-containing complex
B0034394biological_processprotein localization to cell surface
B0034451cellular_componentcentriolar satellite
B0036258biological_processmultivesicular body assembly
B0043001biological_processGolgi to plasma membrane protein transport
B0043231cellular_componentintracellular membrane-bounded organelle
B0045335cellular_componentphagocytic vesicle
B0048227biological_processplasma membrane to endosome transport
B0051650biological_processestablishment of vesicle localization
B0051959molecular_functiondynein light intermediate chain binding
B0055037cellular_componentrecycling endosome
B0055038cellular_componentrecycling endosome membrane
B0060627biological_processregulation of vesicle-mediated transport
B0061502biological_processearly endosome to recycling endosome transport
B0061512biological_processprotein localization to cilium
B0070062cellular_componentextracellular exosome
B0071806biological_processprotein transmembrane transport
B0072594biological_processestablishment of protein localization to organelle
B0072659biological_processprotein localization to plasma membrane
B0090150biological_processestablishment of protein localization to membrane
B0090307biological_processmitotic spindle assembly
B0098837cellular_componentpostsynaptic recycling endosome
B0098887biological_processneurotransmitter receptor transport, endosome to postsynaptic membrane
B0098978cellular_componentglutamatergic synapse
B0150093biological_processamyloid-beta clearance by transcytosis
B1902017biological_processregulation of cilium assembly
B1902954biological_processregulation of early endosome to recycling endosome transport
B1903438biological_processpositive regulation of mitotic cytokinetic process
B1904779biological_processregulation of protein localization to centrosome
B1990182biological_processexosomal secretion
B2001135biological_processregulation of endocytic recycling
E0016301molecular_functionkinase activity
E0046854biological_processphosphatidylinositol phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue GDP B 301
ChainResidue
BSER20
BLEU38
BASN124
BLYS125
BASP127
BLEU128
BSER154
BALA155
BLEU156
BGLY21
BVAL22
BGLY23
BLYS24
BSER25
BASN26
BPHE36
BASN37

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 E 1001
ChainResidue
EHIS605
ELYS608
EASN659

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 E 1002
ChainResidue
ETYR183
ELYS195
EARG232
EGLY233
ELYS235
ELEU236

site_idAC4
Number of Residues13
Detailsbinding site for residue 5S8 E 1003
ChainResidue
ELEU374
EPRO381
EILE547
ELYS549
ETYR583
EILE595
EPRO597
EVAL598
EALA601
EGLY660
EASN661
ELEU663
EILE673

Functional Information from PROSITE/UniProt
site_idPS00915
Number of Residues15
DetailsPI3_4_KINASE_1 Phosphatidylinositol 3- and 4-kinases signature 1. VKcg.DDLRQEllafQ
ChainResidueDetails
EVAL548-GLN562

site_idPS00916
Number of Residues21
DetailsPI3_4_KINASE_2 Phosphatidylinositol 3- and 4-kinases signature 2. ScAgycLvcYLLqVkDRHngN
ChainResidueDetails
ESER641-ASN661

site_idPS00675
Number of Residues14
DetailsSIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VVLiGDSGVGKsnL
ChainResidueDetails
BVAL14-LEU27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:11277933, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ELYS297
BASN124
BSER154

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:11277933
ChainResidueDetails
EASP302
EPRO577
EHIS658

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:11277933, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
EVAL305

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8BKC8
ChainResidueDetails
EILE314
EARG323

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:11277933, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ESER316

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:11277933, ECO:0000269|PubMed:23572552
ChainResidueDetails
ELYS333
BCYS213

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ELEU567

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:11277933, ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ETYR650

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
EASP656

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9UBF8
ChainResidueDetails
EALA294

218853

PDB entries from 2024-04-24

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