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4QMT

MST3 in complex with HESPERADIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE H1N A 401
ChainResidue
AILE30
ATYR101
ALEU102
AGLY103
AGLY104
AASN149
ALEU151
AASP162
ATYR291
AHOH602
AHOH702
AGLY31
AHOH703
AGLY33
ASER34
AVAL38
AALA51
ALYS53
AMET99
AGLU100

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 402
ChainResidue
AASP78
AHOH696

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSFGEVFkGidnrtqkv..........VAIK
ChainResidueDetails
AILE30-LYS53

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsMotif: {"description":"Bipartite nuclear localization signal"}
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 Residues13
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"17046825","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19604147","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20124694","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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