9O0U

MAP2K1 (Dual specificity mitogen-activated protein kinase kinase 1)
RAF1 (RAF proto-oncogene serine/threonine-protein kinase)
Group: STE TKL
Uniprot: RAF1_HUMAN MP2K1_HUMAN
Organism: Homo sapiens
Domain boundary: 68 - 361 349 - 608
Resolution: 2.91

Chain id Group Gene UniprotID Protein Organism Activity Spatial Dihedral Chelix-SaltBridge ActLoopNT-ActLoopCT Ligand Type Residues in structure Unresolved residues in A-loop
B STE MAP2K1 MP2K1_HUMAN Dual specificity mitogen-activated protein kinase kinase 1 Homo sapiens Inactive DFGin BLBplus out-out out-out CHU Type1 30 - 380 0
D STE MAP2K1 MP2K1_HUMAN Dual specificity mitogen-activated protein kinase kinase 1 Homo sapiens Inactive DFGin BLBplus out-out out-out CHU Type3 31 - 380 0
F STE MAP2K1 MP2K1_HUMAN Dual specificity mitogen-activated protein kinase kinase 1 Homo sapiens Inactive DFGin BLBplus out-out out-out CHU Type3 30 - 380 0
H STE MAP2K1 MP2K1_HUMAN Dual specificity mitogen-activated protein kinase kinase 1 Homo sapiens Inactive DFGin BLBplus out-out out-out CHU ANP Type1 Type1 30 - 380 0
A TKL RAF1 RAF1_HUMAN RAF proto-oncogene serine/threonine-protein kinase Homo sapiens Inactive DFGin BLBplus out-none out-out 324 Type1.5_Back 339 - 612 7
C TKL RAF1 RAF1_HUMAN RAF proto-oncogene serine/threonine-protein kinase Homo sapiens Inactive DFGin BLBminus in-in in-out 324 Type1 339 - 614 12
E TKL RAF1 RAF1_HUMAN RAF proto-oncogene serine/threonine-protein kinase Homo sapiens Inactive DFGin BLAplus out-none none-out 324 Type1.5_Back 339 - 613 17
G TKL RAF1 RAF1_HUMAN RAF proto-oncogene serine/threonine-protein kinase Homo sapiens Inactive DFGin BLAminus in-in in-out 324 Type1 341 - 614 9
All chains
Pymol session(ver 2.3) Pymol script
All chains - renumbered by
Uniprot PDB Alignment 
Representative sequence - Chain G
       345        355        365        375 
sdssdDWEIE ASEVMLSTRI GSGSFGTVYK GKWHGDVAVK 
       385        395        405        415 
ILKVVDPTPE QFQAFRNEVA VLRKTRHVNI LLFMGYMTKD 
       425        435        445        455 
NLAIVTQWCE GSSLYKHLHV QETKFQMFQL IDIARQTAQG 
       465        475        485        495 
MDYLHAKNII HRDMKSNNIF LHEGLTVKIG DFGLATVKsr 
       505        515        525        535 
wsgsqqvEQP TGSVLWMAPE VIRMQDNNPF SFQSDVYSYG 
       545        555        565        575 
IVLYELMTGE LPYSHINNRD QIIFMVGRGY ASPDLSKLYK 
       585        595        605        615 
NCPKAMKRLV ADCVKKVKEE RPLFPQILSS IELLQHSLPk


Lower-case residues are disordered in structure.
Mutations: Y340D,Y341D
Phosphorylation: None