3DLS

PASK (PAS domain-containing serine/threonine-protein kinase)
Group: CAMK
Uniprot: PASK_HUMAN
Organism: Homo sapiens
Domain boundary: 999 - 1251
Resolu: 2.3

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 ADP Type1 982 - 1266 0
B Active DFGin BLAminus in-in in-in ADP Type1 982 - 1267 0
C Active DFGin BLAminus in-in in-in ADP Type1 982 - 1267 0
D Active DFGin BLAminus in-in in-in ADP Type1 982 - 1266 0
E Active DFGin BLAminus in-in in-in ADP Type1 982 - 1267 0
F Active DFGin BLAminus in-in in-in ADP Type1 982 - 1266 0
All chains
Pymol session(ver 2.3) Pymol script
All chains - renumbered by
Uniprot PDB Alignment 
Representative sequence - Chain F
       983        993       1003       1013 
maleeppkAV ELEGLAACEG EYSQKYSTMS PLGSGAFGFV 
      1023       1033       1043       1053 
WTAVDKEKNK EVVVKFIKKE KVledcWIED PKLGKVTLEI 
      1063       1073       1083       1093 
AILSRVEHAN IIKVLDIFEN QGFFQLVMEK HGSGLDLFAF 
      1103       1113       1123       1133 
IDRHPRLDEP LASYIFRQLV SAVGYLRLKD IIHRDIKDEN 
      1143       1153       1163       1173 
IVIAEDFTIK LIDFGSAAYL ERGKLFYTFC GTIEYCAPEV 
      1183       1193       1203       1213 
LMGNPYRGPE LEMWSLGVTL YTLVFEENPF CELEETVEAA 
      1223       1233       1243       1253 
IHPPYLVSKE LMSLVSGLLQ PVPERRTTLE KLVTDPWVTQ 
      1263       1273       1283       1293 
PVNLADYTWE EVFrvnkpes gvlsaaslem gnrslsdvaq 
         - 
aqelcggegh hhhhh
Lower-case residues are disordered in structure.
Mutations: None
Phosphorylation: None