3VRY

HCK (Tyrosine-protein kinase HCK)
Group: TYR
Uniprot: HCK_HUMAN
Organism: Homo sapiens
Domain boundary: 262 - 513
Resolu: 2.481

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 BLBplus out-out out-out B43 Type1.5_Back 81 - 526 12
B Inactive DFGin BLBplus out-out out-out B43 Type1.5_Back 81 - 526 12
All chains
Pymol session(ver 2.3) Pymol script
All chains - renumbered by
Uniprot PDB Alignment 
Representative sequence - Chain B
        82         92        102        112 
gamgsgiRII VVALYDYEAI HHEDLSFQKG DQMVVLEESG 
       122        132        142        152 
EWWKARSLAT RKEGYIPSNY VARVDSLETE EWFFKGISRK 
       162        172        182        192 
DAERQLLAPG NMLGSFMIRD SETTKGSYSL SVRDYDPRQG 
       202        212        222        232 
DTVKHYKIRT LDNGGFYISP RSTFSTLQEL VDHYKKGNDG 
       242        252        262        272 
LCQKLSVPCM SSKPQKPWEK DAWEIPRESL KLEKKLGAGQ 
       282        292        302        312 
FGEVWMATYN KHTKVAVKTM KPGSMSVEAF LAEANVMKTL 
       322        332        342        352 
QHDKLVKLHA VVTKEPIYII TEFMAKGSLL DFLKSDEGSK 
       362        372        382        392 
QPLPKLIDFS AQIAEGMAFI EQRNYIHRDL RAANILVSAS 
       402        412        422        432 
LVCKIADFGL ARVIedneyt aregakFPIK WTAPEAINFG 
       442        452        462        472 
SFTIKSDVWS FGILLMEIVT YGRIPYPGMS NPEVIRALER 
       482        492        502        512 
GYRMPRPENC PEELYNIMMR CWKNRPEERP TFEYIQSVLD 
       522 
DFYTATESQY EEIP
Lower-case residues are disordered in structure.
Mutations: Q523E,Q524E,Q525I
Phosphorylation: X522