6SEQ

LMTK3 (Serine/threonine-protein kinase LMTK3)
Group: TYR
Uniprot: LMTK3_HUMAN
Organism: Homo sapiens
Domain boundary: 133 - 410
Resolu: 2.1

Chain id Activity_label Spatial_label Dihedral_label Chelix-SaltBridge ActLoopNT-ActLoopCT Ligand Type Residues in structure Unresolved residues in A-loop
A Inactive DFGout BBAminus in-out out-in No_ligand No_ligand 130 - 413 0
Representative sequence - Chain A
10 20 30 40
mpapgalill aavsasgcla spahpdgfal graplappya
50 60 70 80
vvliscsgll afifllltcl cckrgdvgfk efenpegedc
90 100 110 120
sgeytppaee tsssqslpdv yilplaevsl pmpapqpshs
130 140 150 160
dmttplglsR QHLSYLQEIG SGWFGKVILG EIFSDYTPAQ
170 180 190 200
VVVKELRASA GPLEQRKFIS EAQPYRSLQH PNVLQCLGLC
210 220 230 240
VETLPFLLIM EFCQLGDLKR YLRAQRPPeg lsPELPPRDL
250 260 270 280
RTLQRMGLEI ARGLAHLHSH NYVHSDLALR NCLLTSDLTV
290 300 310 320
RIGDYGLAHS NYKEDYYLTP ERLWIPLRWA APELLGELHG
330 340 350 360
tfMVVDQSRE SNIWSLGVTL WELFEFGAQP YRHLSDEEVL
370 380 390 400
AFVVRQQHVK LARPRLKLPY ADYWYDILQS CWRPPAQRPS
410 420 430 440
ASDLQLQLTY LLSerpprpp pppppprdgp fpwpwppahs
450 460 470 480
aprpgtlssp fplldgfpga dpddvltvte ssrglnlecl
490 500 510 520
wekarrgagr gggapawqpa sappaphanp snpfyealst
530 540 550 560
psvlpvisar spsvsseyyi rleehgsppe plfpndwdpl
570 580 590 600
dpgvpapqap qapsevpqlv setwasplfp aprpfpaqss
610 620 630 640
asgsfllsgw dpegrgaget lagdpaevlg ergtapwvee
650 660 670 680
eeeeeegssp gedssslggg psrrgplpcp lcsregacsc
690 700 710 720
lplergdava gwgghpalgc phppeddssl raergsladl
730 740 750 760
pmappasapp efldplmgaa apqypgrgpp papppppppp
770 780 790 800
rapadpaasp dppsavaspg sglsspgpkp gdsgyetetp
810 820 830 840
fspegafpgg gaaeeegvpr prappeppdp gaprpppdpg
850 860 870 880
plplpgprek ptfvvqvste qllmslredv trnllgekga
890 900 910 920
taretgprka grgpgnrekv pglnrdptvl gngkqapsls
930 940 950 960
lpvngvtvle ngdqrapgie ekaaengalg spereekvle
970 980 990 1000
ngeltpprre ekalengelr speagekvlv nggltppkse
1010 1020 1030 1040
dkvsengglr fprnterppe tgpwrapgpw ektpeswgpa
1050 1060 1070 1080
ptigepapet slerapapsa vvssrngget apgplgpapk
1090 1100 1110 1120
ngtlepgter rapetggapr apgagrldlg sggrapvgtg
1130 1140 1150 1160
tapgggpgsg vdakagwvdn trpqpppppl ppppeaqprr
1170 1180 1190 1200
lepapprarp evapegepga pdsraggdta lsgdgdppkp
1210 1220 1230 1240
erkgpemprl fldlgppqgn seqikarlsr lslalppltl
1250 1260 1270 1280
tpfpgpgprr ppwegadaga aggeaggaga pgpaeedged
1290 1300 1310 1320
ededeeedee aaapgaaagp rgpgraraap vpvvvssada
1330 1340 1350 1360
daarplrgll ksprgadepe dselerkrkm vsfhgdvtvy
1370 1380 1390 1400
lfdqetptne lsvqappegd tdpstppapp tpphpatpgd
1410 1420 1430 1440
gfpsndsgfg gsfewaedfp llpppgpplc fsrfsvspal
1450 1460
etpgpparap darpagpven
Lower-case residues are disordered in structure.
Mutations: None
Phosphorylation: None