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3FPM

Crystal Structure of a Squarate Inhibitor bound to MAPKAP Kinase-2

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 Residues9
DetailsBINDING SITE FOR RESIDUE 793 A 1
ChainResidue
AGLY73
AASN75
AALA91
ALYS93
AMET138
AGLU139
ALEU141
AGLU190
AASP207

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
ALYS93
ALEU70

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
ATHR222

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by MAPK14 => ECO:0000269|PubMed:8846784
ChainResidueDetails
ASER272

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250
ChainResidueDetails
ASER328

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
ATHR334

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:21131586
ChainResidueDetails
ALYS353

221051

PDB entries from 2024-06-12

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