8E04

LRRK1 (Leucine-rich repeat serine/threonine-protein kinase 1)
Group: TKL
Uniprot: LRRK1_HUMAN
Organism: Homo sapiens
Domain boundary: 1238 - 1522
Resolu: 3.8

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-in none-none No_ligand No_ligand 381 - 2007 23
Representative sequence - Chain A
29 39 49 59
savcperame tlngagdtgg kpstrggdpa arsrrtegir
69 79 89 99
aayrrgdrgg ardlleeacd qcasqlekgq llsipaaygd
109 119 129 139
lemvryllsk rlvelptept ddnpavvaay fghtavvqel
149 159 169 179
leslpgpcsp qrllnwmlal acqrghlgvv kllvlthgad
189 199 209 219
pesyavrkne fpvivrlply aaiksgnedi aifllrhgay
229 239 249 259
fcsyilldsp dpskhllrky fieasplpss ypgktalrvk
269 279 289 299
wshlrlpwvd ldwlidiscq iteldlsanc latlpsvipw
309 319 329 339
glinlrklnl sdnhlgelpg vqssdeiics rlleidissn
349 359 369 379
klshlppgfl hlsklqklta skncleklfe eenatnwigl
389 399 409 419
rKLQELDISD NKLTELPALF LHSFKSLNSL NVSRNNLKVF
429 439 449 459
PDPWACPLKC CKASRNALEC LPDKMAVFWK NHLKDVDFSE
469 479 489 499
NALKEVPLGL FQLDALMFLR LQGNQLAALP PQEKWTCRQL
509 519 529 539
KTLDLSRNQL Gknedglktk riaffttrgr qrsgteaasV
549 559 569 579
LEFPAFLSES LEVLCLNDNH LDTVPPSVCL LKSLSELYLG
589 599 609 619
NNPGLRELPP ELGQLGNLWQ LDTEDLTISN VPAEIQKEGP
629 639 649 659
KAMLSYLRAQ LRKAEKCKLM KMIIVGPPRQ GKSTLLEILQ
669 679 689 699
TGRAPQVVHG EATIRTTKWE LQRPagsrak VESVEFNVWD
709 719 729 739
IGGPASMATV NQCFFTDKAL YVVVWNLALG EEAVANLQFW
749 759 769 779
LLNIEAKAPN AVVLVVGTHL DLIeakfrVE RIATLRAYVL
789 799 809 819
ALCRSPSGSR ATGFPDITFK HLHEISCKSL EGQEGLRQLI
829 839 849 859
FHVTCSMKDv gstigCQRLA GRLIPRSYLS LQEAVLAEQQ
869 879 889 899
RRSRDDDVQY LTDRQLEQLV EQTPDNDIKD YEDLQSAISF
909 919 929 939
LIETGTLLHF pdtshglrnl YFLDPIWLSE CLQRIFNIKg
949 959 969 979
srsvaKNGVI RAEDLRMLLV GTGFTQQTEE QYFQFLAKFE
989 999 1009 1019
IALPVANDSY LLPHLLPSKP gldthgmrhp taNTIQRVFK
1029 1039 1049 1059
MSFVPVGFWQ RFIARMLISL AEMDlqlfen kkntksrnrk
1069 1079 1089 1099
vtiYSFTGNQ RNRCSTFRVK RNQTIYWQEG LLVTFDGGYL
1109 1119 1129 1139
SVESSDVNWK KKKSGGMKIV CQSEVRDFSA MAFITDHVNS
1149 1159 1169 1179
LIDQWFPALT ATESDGTPLM EQYVPCPVCE tawaqhtdps
1189 1199 1209 1219
eksedVQYFD MEDCVLTAIE RDFISCPRHP DLPVPLQELV
1229 1239 1249 1259
PELFMTDFPA RLFLENSKLE HSEDEGSVLG QGGSGTVIYR
1269 1279 1289 1299
ARYQGQPVAV KRFHIkkfkn fanvpaDTML RHLRATDAMK
1309 1319 1329 1339
NFSEFRQEAS MLHALQHPCI VALIGISIHP LCFALELAPL
1349 1359 1369 1379
SSLNTVLsen ardsSFIPLG HMLTQKIAYQ IASGLAYLHK
1389 1399 1409 1419
KNIIFCDLKS DNILVWSLDV KEHINIKLSD YGisrqsfhe
1429 1439 1449 1459
galgvegtpg yqapeirpri vYDEKVDMFS YGMVLYELLS
1469 1479 1489 1499
GQRpalghhq lqiAKKLSKG IRPVLGQPEE VQFRRLQALM
1509 1519 1529 1539
MECWDTKPEK RPLALSVVSQ MKDPTFATFM YELCCGKQTA
1549 1559 1569 1579
FFSSQGQEYT VVFWDGKEES RNYTVVNTEK GLMEVQRMCC
1589 1599 1609 1619
PGMKVSCQLQ VQRSLWTATE DQKIYIYTLK gmcPLNTPQQ
1629 1639 1649 1659
ALDTPAVVTC FLAVPVikkn SYLVLAGLAD GLVAVFPVVR
1669 1679 1689 1699
GTPKDSCSYL CSHTANRSKF SIADEDARQN PYPVKAMEVV
1709 1719 1729 1739
NSGSEVWYSN GPGLLVIDCA SLEICRRLEP YMAPSMVTSV
1749 1759 1769 1779
VCSSEGRGEE VVWCLDDKAN SLVMYHSTTY QLCARYFCGV
1789 1799 1809 1819
PSPLRDMFPV RPldteppaa shtanpkvpe gdsiadvsim
1829 1839 1849 1859
yseelgtqil ihqesltdyc smssyssspp rqaarspssl
1869 1879 1889 1899
psspassssv pfstdcedsd mlhtpgaasd rsehdltpmd
1909 1919 1929 1939
getfsQHLQA VKILAVRDLI WVPRRGGDVI VIGLEKDSGA
1949 1959 1969 1979
QRGRVIAVLK ARELTPHGVL VDAAVVAKDT VVCTFENENT
1989 1999 2009
EWCLAVWRGW GAREFDIFYQ SYEELGRLea ctrkrr
Lower-case residues are disordered in structure.
Mutations: None
Phosphorylation: None