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3GNI

Structure of STRAD and MO25

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0007165biological_processsignal transduction
A0010800biological_processpositive regulation of peptidyl-threonine phosphorylation
A0014823biological_processresponse to activity
A0018105biological_processpeptidyl-serine phosphorylation
A0019900molecular_functionkinase binding
A0030018cellular_componentZ disc
A0030295molecular_functionprotein kinase activator activity
A0032991cellular_componentprotein-containing complex
A0034774cellular_componentsecretory granule lumen
A0035556biological_processintracellular signal transduction
A0043539molecular_functionprotein serine/threonine kinase activator activity
A0070062cellular_componentextracellular exosome
A0071476biological_processcellular hypotonic response
A0071902biological_processpositive regulation of protein serine/threonine kinase activity
A0097066biological_processresponse to thyroid hormone
A1901017biological_processnegative regulation of potassium ion transmembrane transporter activity
A1901380biological_processnegative regulation of potassium ion transmembrane transport
A1902554cellular_componentserine/threonine protein kinase complex
A1904813cellular_componentficolin-1-rich granule lumen
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0043539molecular_functionprotein serine/threonine kinase activator activity
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ATP B 1
ChainResidue
AHOH346
BGLY78
BPHE79
BMET83
BTHR98
BARG100
BTHR147
BSER148
BMET150
BASP157
BSER199
AHOH360
BHIS200
BLEU202
BARG215
AHOH365
AHOH370
AHOH376
AHOH401
BILE75
BGLY76
BLYS77

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CIT A 342
ChainResidue
AARG107
AARG152
AARG194
BHIS223

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by LKB1 => ECO:0000269|PubMed:12805220
ChainResidueDetails
BTHR329
BTHR419

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PDB entries from 2024-06-12

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