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3M42

Crystal structure of MAPKAP kinase 2 (MK2) complexed with a tetracyclic ATP site inhibitor

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 Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1
ChainResidue
AHOH17
ASER112
AGLN113
ACYS114
AILE117

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HGF A 365
ChainResidue
AALA91
ALYS93
AMET138
AGLU139
ACYS140
ALEU141
AGLY144
AGLU145
AASN191
ALEU193
AASP207
AHOH9
ALEU70
ALEU72
AGLY73

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGLGINGKVLqIfnkrtqek..........FALK
ChainResidueDetails
ALEU70-LYS93

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDVKpeNLLY
ChainResidueDetails
AILE182-TYR194

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP186

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU70
ALYS93

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AGLU139

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784
ChainResidueDetails
ASER243

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by MAPK14 => ECO:0000269|PubMed:8846784
ChainResidueDetails
AGLU293

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250
ChainResidueDetails
ATRP349

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
AGLU355

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:21131586
ChainResidueDetails

218853

PDB entries from 2024-04-24

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