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9OT6

Cryo-EM structure of the PI4KA complex bound to an EFR3 interfering nanobody (F3IN)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004430molecular_function1-phosphatidylinositol 4-kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0006629biological_processlipid metabolic process
A0006661biological_processphosphatidylinositol biosynthetic process
A0007165biological_processsignal transduction
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0030660cellular_componentGolgi-associated vesicle membrane
A0044788biological_processhost-mediated perturbation of viral process
A0045296molecular_functioncadherin binding
A0046854biological_processphosphatidylinositol phosphate biosynthetic process
A0048015biological_processphosphatidylinositol-mediated signaling
A0070062cellular_componentextracellular exosome
A0140754biological_processreorganization of cellular membranes to establish viral sites of replication
B0000166molecular_functionnucleotide binding
B0004430molecular_function1-phosphatidylinositol 4-kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005925cellular_componentfocal adhesion
B0006629biological_processlipid metabolic process
B0006661biological_processphosphatidylinositol biosynthetic process
B0007165biological_processsignal transduction
B0016020cellular_componentmembrane
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0030660cellular_componentGolgi-associated vesicle membrane
B0044788biological_processhost-mediated perturbation of viral process
B0045296molecular_functioncadherin binding
B0046854biological_processphosphatidylinositol phosphate biosynthetic process
B0048015biological_processphosphatidylinositol-mediated signaling
B0070062cellular_componentextracellular exosome
B0140754biological_processreorganization of cellular membranes to establish viral sites of replication
D0005515molecular_functionprotein binding
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0046854biological_processphosphatidylinositol phosphate biosynthetic process
D0072659biological_processprotein localization to plasma membrane
F0005515molecular_functionprotein binding
F0005829cellular_componentcytosol
F0005886cellular_componentplasma membrane
F0046854biological_processphosphatidylinositol phosphate biosynthetic process
F0072659biological_processprotein localization to plasma membrane
Functional Information from PROSITE/UniProt
site_idPS00063
Number of Residues16
DetailsALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. LARSLAvqRPaSLeKV
ChainResidueDetails
ALEU38-VAL53

site_idPS00915
Number of Residues15
DetailsPI3_4_KINASE_1 Phosphatidylinositol 3- and 4-kinases signature 1. FKvg.DDCRQDmlalQ
ChainResidueDetails
APHE1849-GLN1863

site_idPS00916
Number of Residues21
DetailsPI3_4_KINASE_2 Phosphatidylinositol 3- and 4-kinases signature 2. SmAaysLllFLLqIkDRHngN
ChainResidueDetails
ASER1942-ASN1962

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues376
DetailsDomain: {"description":"PIK helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00878","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsRegion: {"description":"G-loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsRegion: {"description":"Catalytic loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues48
DetailsRegion: {"description":"Activation loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues66
DetailsRepeat: {"description":"TPR 2"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues66
DetailsRepeat: {"description":"TPR 3"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues66
DetailsRepeat: {"description":"TPR 4"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues70
DetailsRepeat: {"description":"TPR 5"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues64
DetailsRepeat: {"description":"TPR 6"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues66
DetailsRepeat: {"description":"TPR 7"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues66
DetailsRepeat: {"description":"TPR 8"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues66
DetailsRepeat: {"description":"TPR 9"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues64
DetailsRepeat: {"description":"TPR 10"}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues66
DetailsRepeat: {"description":"TPR 11"}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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