4D2T

MELK (Maternal embryonic leucine zipper kinase)
Group: CAMK
Uniprot: MELK_HUMAN
Organism: Homo sapiens
Domain boundary: 11 - 263
Resolu: 2.7

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 3I7 Type1 1 - 333 12
B Active DFGin BLAminus in-in in-in 3I7 Type1 1 - 333 6
C Active DFGin BLAminus in-in in-in 3I7 Type1 1 - 333 13
D Active DFGin BLAminus in-in in-in 3I7 Type1 3 - 333 8
All chains
Pymol session(ver 2.3) Pymol script
All chains - renumbered by
Uniprot PDB Alignment 
Representative sequence - Chain D
         -          -         10         20 
mgsshhhhhh ssglvprgsh mkDYDELLKY YELHETIGTG 
        30         40         50         60 
GFAKVKLACH ILTGEMVAIK IMDKNTLGSD LPRIKTEIEA 
        70         80         90        100 
LKNLRHQHIC QLYHVLETAN KIFMVLEYCP GGELFDYIIS 
       110        120        130        140 
QDRLSEEETR VVFRQIVSAV AYVHSQGYAH RDLKPENLLF 
       150        160        170        180 
DEYHKLKLID FGLCAKPKGN KdyhlqaccG ALAYAAPELI 
       190        200        210        220 
QGKSYLGSEA DVWSMGILLY VLMCGFLPFD DDTAAALVAK 
       230        240        250        260 
IMRGKYDVPK WLSPSSILLL QQMLQVDPKK RISMKNLLNH 
       270        280        290        300 
PWIMQDYNYP VEWQSKNPFI HLDDDCVTEL SVHHrnnrQT 
       310        320        330 
MEDLISLWQY DHLTATYLLL LAKKARGKPV RLRlss
Lower-case residues are disordered in structure.
Mutations: T167A,S171A,N213T,V214A,M215A,Y218V,K219A
Phosphorylation: None