2HAK

MARK1 (Serine/threonine-protein kinase MARK1)
Group: CAMK
Uniprot: MARK1_HUMAN
Organism: Homo sapiens
Domain boundary: 60 - 311
Resolu: 2.6

Chain id Activity_label Spatial_label Dihedral_label Chelix-SaltBridge ActLoopNT-ActLoopCT Ligand Type Residues in structure Unresolved residues in A-loop
A Inactive None None in-out out-out No_ligand No_ligand 55 - 371 8
B Inactive None None out-out out-none No_ligand No_ligand 53 - 371 18
C Inactive None None out-out out-none No_ligand No_ligand 53 - 371 9
D Inactive None None out-out out-none No_ligand No_ligand 54 - 371 9
E Inactive None None out-out out-out No_ligand No_ligand 54 - 371 0
F Inactive None None out-out out-out No_ligand No_ligand 54 - 371 0
G Inactive None None in-out out-none No_ligand No_ligand 55 - 371 10
H Inactive None None out-out out-none No_ligand No_ligand 54 - 371 17
Representative sequence - Chain H
53 63 73 83
gnsitsatde QPHIGNYRLQ KTIGKGNFAK VKLARHVLTG
93 103 113 123
REVAVKIIDK TQLNPTSLQK LFREVRIMKI LNHPNIVKLF
133 143 153 163
EVIETEKTLY LVMEYASGGE VFDYLVAHGR MKEKEARAKF
173 183 193 203
RQIVSAVQYC HQKYIVHRDL KAENLLLDGD MNIKIADFGF
213 223 233 243
SNEFTVgnkl dtfcgsppya apelfqgkky dGPEVDVWSL
253 263 273 283
GVILYTLVSG SLPFDgqnlk elrervlrgk yRIPFYMSTD
293 303 313 323
CENLLKKLLV LNPIKRGSLE QIMKDRWMNV GHEEEELKPY
333 343 353 363
TEPDPDFNDT KRIDIMVTMG FARDEINDAL INQKYDEVMA

TYILLGRK
Lower-case residues are disordered in structure.
Mutations: None
Phosphorylation: None