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4OJK

Structure of the cGMP Dependent Protein Kinase II and Rab11b Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
A0031410cellular_componentcytoplasmic vesicle
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
A0098876biological_processvesicle-mediated transport to the plasma membrane
A0150093biological_processamyloid-beta clearance by transcytosis
A2000008biological_processregulation of protein localization to cell surface
A2001135biological_processregulation of endocytic recycling
B0000166molecular_functionnucleotide binding
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
B0031410cellular_componentcytoplasmic vesicle
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
B0098876biological_processvesicle-mediated transport to the plasma 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 Residues30
DetailsBINDING: BINDING => ECO:0000305|PubMed:16545962, ECO:0007744|PDB:2F9M
ChainResidueDetails
ASER20
AGLY69
AASN124
ALYS125
AASP127
AALA155
ALEU156
BSER20
BGLY21
BGLY23
BLYS24
AGLY21
BASN26
BASN37
BLEU38
BSER40
BSER42
BGLY69
BASN124
BLYS125
BASP127
BALA155
AGLY23
BLEU156
ALYS24
AASN26
AASN37
ALEU38
ASER40
ASER42

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:2F9L, ECO:0007744|PDB:2F9M
ChainResidueDetails
ASER25
BSER25

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:2F9M
ChainResidueDetails
ATHR43
AASP66
BTHR43
BASP66

237735

PDB entries from 2025-06-18

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