1WMK

DAPK2 (Death-associated protein kinase 2)
Group: CAMK
Uniprot: DAPK2_HUMAN
Organism: Homo sapiens
Domain boundary: 23 - 285
Resolu: 3.6

Chain id Activity_label Spatial_label Dihedral_label Chelix-SaltBridge ActLoopNT-ActLoopCT Ligand Type Residues in structure Unresolved residues in A-loop
A Inactive DFGin BLAminus in-in in-out No_ligand No_ligand 12 - 314 0
B Inactive DFGin BLAminus in-in in-out No_ligand No_ligand 12 - 325 0
C Inactive DFGin BLAminus in-in in-out No_ligand No_ligand 12 - 314 0
D Inactive DFGin BLAminus in-in in-out No_ligand No_ligand 12 - 325 0
E Inactive DFGin BLAminus in-in in-out No_ligand No_ligand 12 - 324 0
F Inactive DFGin BLAminus in-in in-out No_ligand No_ligand 12 - 314 0
G Inactive DFGin BLAminus in-in in-out No_ligand No_ligand 12 - 324 0
H Inactive DFGin BLAminus in-in in-out No_ligand No_ligand 12 - 315 0
All chains
Pymol session(ver 2.3) Pymol script
All chains - renumbered by
Uniprot PDB Alignment 
Representative sequence - Chain H
        19         29         39         49 
gmEPFKQQKV EDFYDIGEEL GSGQFAIVKK CREKSTGLEY 
        59         69         79         89 
AAKFIKKRQS RASRRGVSRE EIEREVSILR QVLHHNVITL 
        99        109        119        129 
HDVYENRTDV VLILELVSGG ELFDFLAQKE SLSEEEATSF 
       139        149        159        169 
IKQILDGVNY LHTKKIAHFD LKPENIMLLD KNIPIPHIKL 
       179        189        199        209 
IDFGLAHEIE DGVEFKNIFG TPEFVAPEIV NYEPLGLEAD 
       219        229        239        249 
MWSIGVITYI LLSGASPFLG DTKQETLANI TAVSYDFDEE 
       259        269        279        289 
FFSQTSELAK DFIRKLLVKE TRKRLTIQEA LRHPWITPVD 
       299        309        319        329 
NQQAMVRRES VVNLENFRKQ YVRRRWkldf sivslcnhlt 

r
Lower-case residues are disordered in structure.
Mutations: S318D
Phosphorylation: None