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4OJK

Structure of the cGMP Dependent Protein Kinase II and Rab11b Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0001881biological_processreceptor recycling
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0008021cellular_componentsynaptic vesicle
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019003molecular_functionGDP binding
A0030670cellular_componentphagocytic vesicle membrane
A0030672cellular_componentsynaptic vesicle membrane
A0031489molecular_functionmyosin V binding
A0032402biological_processmelanosome transport
A0032456biological_processendocytic recycling
A0033572biological_processtransferrin transport
A0035773biological_processinsulin secretion involved in cellular response to glucose stimulus
A0044070biological_processregulation of monoatomic anion transport
A0045054biological_processconstitutive secretory pathway
A0045055biological_processregulated exocytosis
A0045202cellular_componentsynapse
A0045296molecular_functioncadherin binding
A0045335cellular_componentphagocytic vesicle
A0055037cellular_componentrecycling endosome
A0055038cellular_componentrecycling endosome membrane
A0070062cellular_componentextracellular exosome
A0071468biological_processcellular response to acidic pH
A0090150biological_processestablishment of protein localization to membrane
A0150093biological_processamyloid-beta clearance by transcytosis
A2000008biological_processregulation of protein localization to cell surface
A2001135biological_processregulation of endocytic recycling
B0001881biological_processreceptor recycling
B0003924molecular_functionGTPase activity
B0003925molecular_functionG protein activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005768cellular_componentendosome
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0008021cellular_componentsynaptic vesicle
B0015031biological_processprotein transport
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0019003molecular_functionGDP binding
B0030670cellular_componentphagocytic vesicle membrane
B0030672cellular_componentsynaptic vesicle membrane
B0031489molecular_functionmyosin V binding
B0032402biological_processmelanosome transport
B0032456biological_processendocytic recycling
B0033572biological_processtransferrin transport
B0035773biological_processinsulin secretion involved in cellular response to glucose stimulus
B0044070biological_processregulation of monoatomic anion transport
B0045054biological_processconstitutive secretory pathway
B0045055biological_processregulated exocytosis
B0045202cellular_componentsynapse
B0045296molecular_functioncadherin binding
B0045335cellular_componentphagocytic vesicle
B0055037cellular_componentrecycling endosome
B0055038cellular_componentrecycling endosome membrane
B0070062cellular_componentextracellular exosome
B0071468biological_processcellular response to acidic pH
B0090150biological_processestablishment of protein localization to membrane
B0150093biological_processamyloid-beta clearance by transcytosis
B2000008biological_processregulation of protein localization to cell surface
B2001135biological_processregulation of endocytic recycling
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GDP A 301
ChainResidue
AASP19
ALEU38
AGLU39
ALYS41
AARG74
AALA75
AASN124
ALYS125
AASP127
ALEU128
ASER154
AGLY21
AALA155
ALEU156
AHOH401
AVAL22
AGLY23
ALYS24
ASER25
AASN26
APHE36
AASN37

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GDP B 301
ChainResidue
BASP19
BGLY21
BVAL22
BGLY23
BLYS24
BSER25
BASN26
BPHE36
BASN37
BLEU38
BGLU39
BASN124
BLYS125
BASP127
BSER154
BALA155
BLEU156

Functional Information from PROSITE/UniProt
site_idPS00675
Number of Residues14
DetailsSIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VVLiGDSGVGKsnL
ChainResidueDetails
AVAL14-LEU27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16545962
ChainResidueDetails
AGLY18
AASP66
AASN124
ASER154
BGLY18
BASP66
BASN124
BSER154

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PDB entries from 2024-06-12

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