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4FZA

Crystal structure of MST4-MO25 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0007165biological_processsignal transduction
A0014823biological_processresponse to activity
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
A0097066biological_processresponse to thyroid hormone
A0120283molecular_functionprotein serine/threonine kinase binding
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 Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 301
ChainResidue
BSER34
BASP144
BLYS146
BPHE179
BGLY181

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 302
ChainResidue
BPHE163
BGOL303
BTHR83
BGLU100
BALA161
BALA162

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 303
ChainResidue
BVAL38
BLYS53
BPHE163
BGOL302
BHOH1008

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues250
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"29232556","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"15037601","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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