5W5O

RIPK2 (Receptor-interacting serine/threonine-protein kinase 2)
Group: TKL
Uniprot: RIPK2_HUMAN
Organism: Homo sapiens
Domain boundary: 18 - 292
Resolu: 2.89

Chain id Activity_label Spatial_label Dihedral_label Chelix-SaltBridge ActLoopNT-ActLoopCT Ligand Type Residues in structure Unresolved residues in A-loop
A None DFGin BLAminus in-none in-out 9XA Type1 5 - 310 15
B None DFGin BLAminus in-none in-out 9XA Type1 5 - 310 15
C None DFGin BLAminus in-none in-out 9XA Type1 5 - 310 15
D None DFGin BLAminus in-none in-out 9XA Type1 5 - 310 15
E Inactive DFGin BLAminus in-in in-out 9XA Type1 5 - 310 15
F None DFGin BLAminus in-none in-out 9XA Type1 5 - 310 15
G None DFGin BLAminus in-none in-out 9XA Type1 5 - 310 15
H Inactive DFGin BLAminus in-in in-out 9XA Type1 5 - 310 15
I None DFGin BLAminus in-none in-out 9XA Type1 5 - 310 15
J Inactive DFGin BLAminus in-in in-out 9XA Type1 5 - 310 15
K Inactive DFGin BLAminus in-in in-out 9XA Type1 5 - 310 15
L Inactive DFGin BLAminus in-in in-out 9XA Type1 5 - 310 15
M None DFGin BLAminus in-none in-out 9XA Type1 5 - 310 15
N None DFGin BLAminus in-none in-out 9XA Type1 5 - 310 15
O Inactive DFGin BLAminus in-in in-out 9XA Type1 5 - 310 15
P None DFGin BLAminus in-none in-out 9XA Type1 5 - 310 15
All chains
Pymol session(ver 2.3) Pymol script
All chains - renumbered by
Uniprot PDB Alignment 
Representative sequence - Chain P
        11         21         31         41 
ngeAICSALP TIPYHKLADL RYLSRGASGT VSSARHADWR 
        51         61         71         81 
VQVAVKHlhi htplldSERK DVLREAEILH KARFSYILPI 
        91        101        111        121 
LGICNEPEFL GIVTEYMPNG SLNELLHRKT EYPDVAWPLR 
       131        141        151        161 
FRILHEIALG VNYLHNMTPP LLHHDLKTQN ILLDNEFHVK 
       171        181        191        201 
IADFGLSKWR Mmslsqsrss ksapegGTII YMPPENYEPg 
       211        221        231        241 
qksrasIKHD IYSYAVITWE VLSRKQPFED VTNPLQIMYS 
       251        261        271        281 
VSQGHRPVIN EESLPYDIPH RARMISLIES GWAQNPDERP 
       291        301        311 
SFLKCLIELE PVLRTFEEIT FLEAVIQLKk
Lower-case residues are disordered in structure.
Mutations: None
Phosphorylation: None