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3FYK

Crystal structure of a benzthiophene lead bound to MAPKAP Kinase-2 (MK-2)

Functional Information from GO Data
ChainGOidnamespacecontents
X0004672molecular_functionprotein kinase activity
X0005524molecular_functionATP binding
X0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE B98 X 372
ChainResidue
XGLY71
XTHR206
XASP207
XGLY73
XALA91
XLYS93
XMET138
XGLU139
XLEU141
XGLU190
XASN191

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGLGINGKVLqIfnkrtqek..........FALK
ChainResidueDetails
XLEU70-LYS93

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDVKpeNLLY
ChainResidueDetails
XILE182-TYR194

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
XASP186

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
XLEU70
XLYS93

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
XGLU139

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784
ChainResidueDetails
XTHR222

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by MAPK14 => ECO:0000269|PubMed:8846784
ChainResidueDetails
XSER272

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250
ChainResidueDetails
XSER328

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
XTHR334

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:21131586
ChainResidueDetails
XLYS353

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
XASP186
XGLU190

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
XASP186
XLYS188

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
XASP186
XASN191
XLYS188

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PDB entries from 2024-07-10

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