3QA8

IKBKBL (IkappaB kinase)
Group: OTHER
Uniprot: Q6INT1_XENLA
Organism: Xenopus laevis
Domain boundary: 1 - 291
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 DFGout None in-in out-out No_ligand No_ligand 1 - 650 0
B Inactive DFGout None in-in out-out No_ligand No_ligand 1 - 650 0
C Inactive DFGout None in-in out-out No_ligand No_ligand 1 - 650 0
D Inactive DFGout None in-in out-out No_ligand No_ligand 1 - 650 0
E Inactive DFGout None in-in out-out No_ligand No_ligand 1 - 650 0
F Inactive DFGout None in-in out-out No_ligand No_ligand 1 - 650 0
G Inactive DFGout None in-in out-out No_ligand No_ligand 1 - 621 0
H Inactive DFGout None in-in out-out No_ligand No_ligand 1 - 621 0
All chains
Pymol session(ver 2.3) Pymol script
All chains - renumbered by
Uniprot PDB Alignment 
Representative sequence - Chain H
         -          3         13         23 
gggrspslpt qtcgpwEMKE RLGTGGFGYV LRWIHQDTGE 
        33         43         53         63 
QVAIKQCRQE LSPKNRERWC LEIQIMKKLN HPNVVSAREV 
        73         83         93        103 
PDGLQKLAPN DLPLLAMEYC EGGDLRKYLN QFENCCGLKE 
       113        123        133        143 
GPIRTLLSDI SSALRYLHEN RIIHRDLKPE NIVLQPGPQR 
       153        163        173        183 
LIHKIIDLGY AKELDQGELC TEFVGTLQYL APELLEQKKY 
       193        203        213        223 
TVTVDYWSFG TLAFECITGF RPFLPNWQPV QWHGKVReks 
       233        243        253        263 
nehIVVYDDL TGAVKFSSVL PTPNHLSGIL AGKLERWLQC 
       273        283        293        303 
MLMWHQRqrg TDPQNPNVGC FQALDSILSL KLLSVMNMVS 
       313        323        333        343 
GRVHTYPVTE NENLQNLKSW LQQDTGIPEE EQELLQASGL 
       353        363        373        383 
ALNSAQPLTQ YVIDCTVidg rqgeGDLIFL FDNRKtvyep 
       393        403        413        423 
qISLPAHPES VSIVLQDPKR PLTYTHLRRV WGQIWQTIRA 
       433        443        453        463 
LKEDCARLLQ GQRTSMVNLL RYNTELSKKK NSMTSEceql 
       473        483        493        503 
kakldffrss iqidlekyse qmefgitsek llsawremeq 
       513        523        533        543 
avelcgreRE VQALVDKMMA LQTDSVDLQR NPlgrkhrgT 
       553        563        573        583 
LDDLEEQARD LYRRLRERPR DQRTPGDSND MVRLLILAIQ 
       593        603        613        623 
SFEKRVILIY DQLSKTVVCK RKALELSPKV KEVMNLMRed 
       633        643        653 
ekivvrrqek rqqelwnllk iacskvrgpv sgspds
Lower-case residues are disordered in structure.
Mutations: S161E,S165E
Phosphorylation: None