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3FXW

High resolution crystal structure of mitogen-activated protein kinase-activated protein kinase 3/inhibitor 2 complex

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 Residues14
DetailsBINDING SITE FOR RESIDUE F10 A 1
ChainResidue
ALEU50
ALEU173
ATHR186
AASP187
AHOH432
AHOH433
ALEU52
AVAL58
AALA71
ALYS73
AGLU119
ACYS120
AMET121
AGLU122

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGLGVNGKVLeCfhrrtgqk..........CALK
ChainResidueDetails
ALEU50-LYS73

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDVKpeNLLY
ChainResidueDetails
AILE162-TYR174

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP166

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU50
ALYS73

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAPK14 => ECO:0000250|UniProtKB:Q3UMW7
ChainResidueDetails
ATHR201

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by MAPK14 => ECO:0000250
ChainResidueDetails
ASER251

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250
ChainResidueDetails
ASER307

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAPK14 => ECO:0000250
ChainResidueDetails
ATHR313

226707

PDB entries from 2024-10-30

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