6TCA

MAPK14 (Mitogen-activated protein kinase 14)
MAPKAPK2 (MAP kinase-activated protein kinase 2)
Group: CMGC CAMK
Uniprot: MAPK2_HUMAN MK14_HUMAN
Organism: Homo sapiens
Domain boundary: 63 - 325 24 - 308
Resolution: 3.7

Chain id Group Gene UniprotID Protein Organism Activity Spatial Dihedral Chelix-SaltBridge ActLoopNT-ActLoopCT Ligand Type Residues in structure Unresolved residues in A-loop
A CAMK MAPKAPK2 MAPK2_HUMAN MAP kinase-activated protein kinase 2 Homo sapiens Inactive DFGin BLAminus out-out in-out No_ligand No_ligand 51 - 399 0
C CAMK MAPKAPK2 MAPK2_HUMAN MAP kinase-activated protein kinase 2 Homo sapiens Inactive DFGin BLAminus out-out in-out No_ligand No_ligand 51 - 397 0
E CAMK MAPKAPK2 MAPK2_HUMAN MAP kinase-activated protein kinase 2 Homo sapiens None DFGin BLAminus out-none in-out No_ligand No_ligand 51 - 394 0
G CAMK MAPKAPK2 MAPK2_HUMAN MAP kinase-activated protein kinase 2 Homo sapiens None DFGin BLAminus out-none in-out No_ligand No_ligand 51 - 397 0
B CMGC MAPK14 MK14_HUMAN Mitogen-activated protein kinase 14 Homo sapiens Inactive DFGin BLAminus out-out in-in 39G Type1.5_Back 6 - 354 0
D CMGC MAPK14 MK14_HUMAN Mitogen-activated protein kinase 14 Homo sapiens Inactive DFGin BLAminus out-out in-in 39G Type1.5_Back 4 - 353 0
F CMGC MAPK14 MK14_HUMAN Mitogen-activated protein kinase 14 Homo sapiens Inactive DFGin BLAminus out-out in-in 39G Type1.5_Back 6 - 353 0
H CMGC MAPK14 MK14_HUMAN Mitogen-activated protein kinase 14 Homo sapiens Inactive DFGin BLAminus out-out in-in 39G Type1.5_Back 4 - 353 0
All chains
Pymol session(ver 2.3) Pymol script
All chains - renumbered by
Uniprot PDB Alignment 
Representative sequence - Chain H
         6         16         26         36 
gsasmsqERP TFYRQELNKT IWEVPERYQN LSPVGSgayg 
        46         56         66         76 
SVCAAFDTKT GLRVAVKKLS RPFQSIIHAK RTYRELRLLK 
        86         96        106        116 
HMKHENVIGL LDVFTPARSL EEFNDVYLVT HLMGADLNNI 
       126        136        146        156 
VKCQKLTDDH VQFLIYQILR GLKYIHSADI IHRDLKPSNL 
       166        176        186        196 
AVNEDCELKI LDFGLARHTD DEMTGYVATR WYRAPEIMLN 
       206        216        226        236 
WMHYNQTVDI WSVGCIMAEL LTGRTLFPGT DHIDQLKLIL 
       246        256        266        276 
RLVGTPGAEL LKKISSESAR NYIQSLTQMP KMNFANVFIG 
       286        296        306        316 
ANPLAVDLLE KMLVLDSDKR ITAAQALAHA YFAQYHDPDD 
       326        336        346        356 
EPVADPYDQS FESRDLLIDE WKSLTYDEVI SFVPPPLdqe 

emes
Lower-case residues are disordered in structure.
Mutations: None
Phosphorylation: X180,X182