8E06

LRRK1 (Leucine-rich repeat serine/threonine-protein kinase 1)
Group: TKL
Uniprot: LRRK1_HUMAN
Organism: Homo sapiens
Domain boundary: 1238 - 1522
Resolu: 4.3

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 None in-out none-none No_ligand No_ligand 51 - 2007 22
Representative sequence - Chain A
9 19 29 39
smagmsqrpp smywcvgpee savcperame tlngagdtgg
49 59 69 79
kpstrggdpa aRSRRTEGIR AAYRRGDRGG ARDLLEEACD
89 99 109 119
QCASQLEKGQ LLSIPAAYGD LEMVRYLLSK RLVELPTEPT
129 139 149 159
DDNPAVVAAY FGHTAVVQEL LESLPGPCSP QRLLNWMLAL
169 179 189 199
ACQRGHLGVV KLLVLTHGAD PESYAVRKNE FPVIVRLPLY
209 219 229 239
AAIKSGNEDI AIFLLRHGAY FCSYILLDSP DPSKHLLRKY
249 259 269 279
FIEASplpss ypgkTALRVK WSHLRLPWVD LDWLIDISCQ
289 299 309 319
ITELDLSANC LATLPSVIPW GLINLRKLNL SDNHLGELPG
329 339 349 359
VQSSDEIICS RLLEIDISSN KLSHLPPGFL HLSKLQKLTA
369 379 389 399
SKNCLEKLFE EENATNWIGL RKLQELDISD NKLTELPALF
409 419 429 439
LHSFKSLNSL NVSRNNLKVF PDPWACPLKC CKASRNALEC
449 459 469 479
LPDKMAVFWK NHLKDVDFSE NALKEVPLGL FQLDALMFLR
489 499 509 519
LQGNQLAALP PQEKWTCRQL KTLDLSRNQL Gknedglktk
529 539 549 559
riaffttrgr qrsgteaasV LEFPAFLSES LEVLCLNDNH
569 579 589 599
LDTVPPSVCL LKSLSELYLG NNPGLRELPP ELGQLGNLWQ
609 619 629 639
LDTEDLTISN VPAEIQKEGP KAMLSYLRAQ LRKAEKCKLM
649 659 669 679
KMIIVGPPRQ GKSTLLEILQ TGRAPQVVHG EATIRTTKWE
689 699 709 719
LQRPAGSRAK VESVEFNVWD IGGPASMATV NQCFFTDKAL
729 739 749 759
YVVVWNLALG EEAVANLQFW LLNIEAKAPN AVVLVVGTHL
769 779 789 799
DLIEAKFRVE RIATLRAYVL ALCRSPSGSR ATGFPDITFK
809 819 829 839
HLHEISCKSL EGQEGLRQLI FHVTCSMKDv gstigCQRLA
849 859 869 879
GRLIPRSYLS LQEAVLAEQQ RRSRDDDVQY LTDRQLEQLV
889 899 909 919
EQTPDNDIKD YEDLQSAISF LIETGTLLHF PDTSHGLRNL
929 939 949 959
YFLDPIWLSE CLQRIFNIKG SRSVAKNGVI RAEDLRMLLV
969 979 989 999
GTGFTQQTEE QYFQFLAKFE IALPVANDSY LLPHLLPSKP
1009 1019 1029 1039
GLDTHGMRHP TANTIQRVFK MSFVPVGFWQ RFIARMLISL
1049 1059 1069 1079
AEMDLQLFen kkntksrnrk vTIYSFTGNQ RNRCSTFRVK
1089 1099 1109 1119
RNQTIYWQEG LLVTFDGGYL SVESSDVNWK KKKSGGMKIV
1129 1139 1149 1159
CQSEVRDFSA MAFITDHVNS LIDQWFPALT ATESDGTPLM
1169 1179 1189 1199
EQYVPCPVCE TAWAqhtdps ekSEDVQYFD MEDCVLTAIE
1209 1219 1229 1239
RDFISCPRHP DLPVPLQELV PELFMTDFPA RLFLENSKLE
1249 1259 1269 1279
HSEDEGSVLG QGGSGTVIYR ARYQGQPVAV KRFHIKKFkn
1289 1299 1309 1319
fanvpADTML RHLRATDAMK NFSEFRQEAS MLHALQHPCI
1329 1339 1349 1359
VALIGISIHP LCFALELAPL SSLNTVLSEN ARDSSFIPLG
1369 1379 1389 1399
HMLTQKIAYQ IASGLAYLHK KNIIFCDLKS DNILVWSLDV
1409 1419 1429 1439
KEHINIKLSD YGIsrqsfhe galgvegtpg yqapeirprI
1449 1459 1469 1479
VYDEKVDMFS YGMVLYELLS GQRPALGHHQ LQIAKKLSKG
1489 1499 1509 1519
IRPVLGQPEE VQFRRLQALM MECWDTKPEK RPLALSVVSQ
1529 1539 1549 1559
MKDPTFATFM YELCCGKQTA FFSSQGQEYT VVFWDGKEES
1569 1579 1589 1599
RNYTVVNTEK GLMEVQRMCC PGMKVSCQLQ VQRSLWTATE
1609 1619 1629 1639
DQKIYIYTLK GMCPLNTPQQ ALDTPAVVTC FLAVPVIKKN
1649 1659 1669 1679
SYLVLAGLAD GLVAVFPVVR GTPKDSCSYL CSHTANRSKF
1689 1699 1709 1719
SIADEDARQN PYPVKAMEVV NSGSEVWYSN GPGLLVIDCA
1729 1739 1749 1759
SLEICRRLEP YMAPSMVTSV VCSSEGRGEE VVWCLDDKAN
1769 1779 1789 1799
SLVMYHSTTY QLCARYFCGV PSPLRDMFPV RPldteppaa
1809 1819 1829 1839
shtanpkvpe gdsiadvsim yseelgtqil ihqesltdyc
1849 1859 1869 1879
smssyssspp rqaarspssl psspassssv pfstdcedsd
1889 1899 1909 1919
mlhtpgaasd rsehdltpmd getFSQHLQA VKILAVRDLI
1929 1939 1949 1959
WVPRRGGDVI VIGLEKDSGA QRGRVIAVLK ARELTPHGVL
1969 1979 1989 1999
VDAAVVAKDT VVCTFENENT EWCLAVWRGW GAREFDIFYQ
2009
SYEELGRLea ctrkrr
Lower-case residues are disordered in structure.
Mutations: None
Phosphorylation: None