8CHF

MAP2K1 (Dual specificity mitogen-activated protein kinase kinase 1)
RAF1 (RAF proto-oncogene serine/threonine-protein kinase)
Group: STE TKL
Uniprot: MP2K1_HUMAN RAF1_HUMAN
Organism: Homo sapiens
Domain boundary: 68 - 361 349 - 608
Resolution: 4.25

Chain id Group Gene UniprotID Protein Organism Activity Spatial Dihedral Chelix-SaltBridge ActLoopNT-ActLoopCT Ligand Type Residues in structure Unresolved residues in A-loop
E STE MAP2K1 MP2K1_HUMAN Dual specificity mitogen-activated protein kinase kinase 1 Homo sapiens Inactive DFGin BLBminus out-out out-out No_ligand No_ligand 62 - 379 0
F STE MAP2K1 MP2K1_HUMAN Dual specificity mitogen-activated protein kinase kinase 1 Homo sapiens Inactive DFGin BLBminus out-out out-out No_ligand No_ligand 62 - 379 0
A TKL RAF1 RAF1_HUMAN RAF proto-oncogene serine/threonine-protein kinase Homo sapiens Inactive DFGin None in-out in-out 29L Type1 341 - 626 6
B TKL RAF1 RAF1_HUMAN RAF proto-oncogene serine/threonine-protein kinase Homo sapiens Inactive DFGin None in-out in-out 29L Type1 341 - 626 6
Representative sequence - Chain B
10 20 30 40
mehiqgawkt isngfgfkda vfdgsscisp tivqqfgyqr
50 60 70 80
rasddgkltd psktsntirv flpnkqrtvv nvrngmslhd
90 100 110 120
clmkalkvrg lqpeccavfr llhehkgkka rldwntdaas
130 140 150 160
ligeelqvdf ldhvpltthn farktflkla fcdicqkfll
170 180 190 200
ngfrcqtcgy kfhehcstkv ptmcvdwsni rqlllfpnst
210 220 230 240
igdsgvpalp sltmrrmres vsrmpvssqh rystphaftf
250 260 270 280
ntsspssegs lsqrqrstst pnvhmvsttl pvdsrmieda
290 300 310 320
irshsesasp salssspnnl sptgwsqpkt pvpaqrerap
330 340 350 360
vsgtqeknki rprgqrdssy DWEIEASEVM LSTRIGSGSF
370 380 390 400
GTVYKGKWHG DVAVKILKVV DPTPEQFQAF RNEVAVLRKT
410 420 430 440
RHVNILLFMG YMTKDNLAIV TQWCEGSSLY KHLHVQETKF
450 460 470 480
QMFQLIDIAR QTAQGMDYLH AKNIIHRDMK SNNIFLHEGL
490 500 510 520
TVKIGDFGLA TVKSRwsgsq qVEQPTGSVL WMAPEVIRMQ
530 540 550 560
DNNPFSFQSD VYSYGIVLYE LMTGELPYSH INNRDQIIFM
570 580 590 600
VGRGYASPDL SKLYKNCPKA MKRLVADCVK KVKEERPLFP
610 620 630 640
QILSSIELLQ HSLPKINRSA SEPSLHraah tedinactlt

tsprlpvf
Lower-case residues are disordered in structure.
Mutations: Y341D
Phosphorylation: X621