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4LG4

Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
E0004672molecular_functionprotein kinase activity
E0005524molecular_functionATP binding
E0006468biological_processprotein phosphorylation
F0004672molecular_functionprotein kinase activity
F0005524molecular_functionATP binding
F0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 401
ChainResidue
AARG145
AGLY169
AGLY197
ATYR198

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 402
ChainResidue
AASN115
AGLU216
AHOH557

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
AGLU100
AASP164
AGOL404
AVAL83
AMET99

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 404
ChainResidue
AVAL41
ACYS102
AGLY105
AGOL403

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGSYGSVFkAihkesgqv..........VAIK
ChainResidueDetails
ALEU33-LYS56

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29063833","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6AO5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsModified residue: {"description":"Phosphothreonine; by PKB/AKT1","evidences":[{"source":"PubMed","id":"20086174","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"23972470","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"23972470","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29063833","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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