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4O27

Crystal structure of MST3-MO25 complex with WIF motif

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
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP B 500
ChainResidue
BGLY33
BASN149
BLEU151
BASP162
BMN501
BSER34
BPHE35
BVAL38
BALA51
BLYS53
BGLU100
BLEU102
BSER106

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN B 501
ChainResidue
BASN149
BASP162
BADP500

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSFGEVFkGidnrtqkv..........VAIK
ChainResidueDetails
BILE30-LYS53

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BASP144

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
BILE30
BLYS53
BGLU100
BASN149
BASP162

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17046825, ECO:0000269|PubMed:19604147, ECO:0000269|PubMed:20124694, ECO:0007744|PubMed:23186163
ChainResidueDetails
BGLU178

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PDB entries from 2024-07-31

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