6BP0

VRK1 (Serine/threonine-protein kinase VRK1)
Group: CK1
Uniprot: VRK1_HUMAN
Organism: Homo sapiens
Domain boundary: 37 - 326
Resolu: 1.9

Chain id Activity_label Spatial_label Dihedral_label Chelix-SaltBridge ActLoopNT-ActLoopCT Ligand Type Residues in structure Unresolved residues in A-loop
A Active DFGin BLAminus in-in in-in No_ligand No_ligand 20 - 341 0
B Active DFGin BLAminus in-in in-in E1D Type1 23 - 341 0
C Active DFGin BLAminus in-in in-in No_ligand No_ligand 21 - 341 0
D Active DFGin BLAminus in-in in-in E1D Type1.5_Back 22 - 341 0
All chains
Pymol session(ver 2.3) Pymol script
All chains - renumbered by
Uniprot PDB Alignment 
Representative sequence - Chain D
        10         20         30         40 
smrvkaaqag rqssakrhla eQFAVGEIIT DMAAAAWKVG 
        50         60         70         80 
LPIgqggfgC IYLADMNsse SVGSDAPCVV KVEPSDNGPL 
        90        100        110        120 
FTELKFYQRA AKPEQIQKWI RTRKLKYLGV PKYWGSGLHD 
       130        140        150        160 
KNGKSYRFMI MDRFGSDLQK IYEANAKRFS RKTVLQLSLR 
       170        180        190        200 
ILDILEYIHE HEYVHGDIKA SNLLLNYKNP DQVYLVDYGL 
       210        220        230        240 
AYRYCPEGVH KAYAADPKRC HDGTIEFTSI DAHNGVAPSR 
       250        260        270        280 
RGDLEILGYC MIQWLTGHLP WEDNLKDPKY VRDSKIRYRE 
       290        300        310        320 
NIASLMDKCF PAANAPGEIA KYMETVKLLD YTEKPLYENL 
       330        340        350        360 
RDILLQGLKA IGSKDDGKLD Lsvvengglk aktitkkraa 

eiee
Lower-case residues are disordered in structure.
Mutations: K34A,K35A,E36A,E212A,K214A,E215A,E292A,K293A,K295A,K359A,K360A
Phosphorylation: None