eF-site ID 6jmq-ABCD
PDB Code 6jmq
Chain A, B, C, D

click to enlarge
Title LAT1-CD98hc complex bound to MEM-108 Fab
Classification MEMBRANE PROTEIN/IMMUNE SYSTEM
Compound Large neutral amino acids transporter small subunit 1
Source (6JMQ)
Sequence A:  ITLLNGVAIIVGTIIGSGIFVTPTGVLKEAGSPGLALVVW
AACGVFSIVGALCYAELGTTISKSGGDYAYMLEVYGSLPA
FLKLWIELLIIRPSSQYIVALVFATYLLKPLFPTCPVPEE
AAKLVACLCVLLLTAVNCYSVKAATRVQDAFAAAKLLALA
LIILLGFVQIFSFEGTKLDVGNIVLALYSGLFAYGGWNYL
NFVTEEMINPYRNLPLAIIISLPIVTLVYVLTNLAYFTTL
STEQMLSSEAVAVDFGNYHLGVMSWIIPVFVGLSCFGSVN
GSLFTSSRLFFVLLTPVPSLVFTCVMTLLYAFSKDIFSVI
NFFSFFNWLCVALAIIGMIWLRHRKPELERPIKVNLALPV
FFILACLFLIAVSFWKTPVECGIGFTIILSGLPVYFFGVW
WKN
B:  RTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPAQKWW
HTGALYRIGDLQAFQGHGAGNLAGLKGRLDYLSSLKVKGL
VLGPIHKNQKDDVAQTDLLQIDPNFGSKEDFDSLLQSAKK
KSIRVILDLTPNYRGENSWFSTQVDTVATKVKDALEFWLQ
AGVDGFQVRDIENLKDASSFLAEWQNITKGFSEDRLLIAG
TNSSDLQQILSLLESNKDLLLTSSYLSDSGSTGEHTKSLV
TQYLNATGNRWCSWSLSQARLLTSFLPAQLLRLYQLMLFT
LPGTPVFSYGDEIGLDAAALPGQPMEAPVMLWDESSFPDI
PGAVSANMTVKGQSEDPGSLLSLFRRLSDQRSKERSLLHG
DFHAFSAGPGLFSYIRHWDQNERFLVVLNFGDVGLSAGLQ
ASDLPASASLPAKADLLLSTQPGREEGSPLELERLKLEPH
EGLLLRFPYAA
C:  QVQLKESGPGLVAPSQSLSITCTVSGFPLTXXXXXWVRQP
PGKGLEWLGXXXXXXXXXXXXXXXXRLSISKDNSKSQVFL
KMNSLQTDDTARYYCARXXXXXXXXXXWGQGTSVTVSSAK
TTPPSVYPLAPGSSMVTLGCLVKGYFPEPVTVTWNSGSLS
SGVHTFPAVLQSDLYTLSSSVTVPSSTWPSETVTCNVAHP
ASSTKVDKKIVPRD
D:  DIVMSQSPSSLVVSVGEKVTMSCXXXXXXXXXXXXXXXXX
WYQQKPGQSPKLLIYXXXXXXXGVPDRFTGSGSGTDFTLT
ISSVKAEDLAVYYCXXXXXXXXXFGGGTKLEIKRADAAPT
VSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSE
RQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTC
EATHKTSTSPIVKSFNRNE
Description (1)  Large neutral amino acids transporter small subunit 1, 4F2 cell-surface antigen heavy chain, Antibody


Functional site
1) chain B
residue 185-205
type TRANSMEM
sequence LLLLFWLGWLGMLAGAVVIIV
description Helical; Signal-anchor for type II membrane protein => ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI2
2) chain A
residue 396-416
type TRANSMEM
sequence VINFFSFFNWLCVALAIIGMI
description Helical; Signal-anchor for type II membrane protein => ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI2
3) chain A
residue 431-451
type TRANSMEM
sequence VNLALPVFFILACLFLIAVSF
description Helical; Signal-anchor for type II membrane protein => ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI2
4) chain A
residue 458-478
type TRANSMEM
sequence CGIGFTIILSGLPVYFFGVWW
description Helical; Signal-anchor for type II membrane protein => ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI2
5) chain A
residue 84-104
type TRANSMEM
sequence LALVVWAACGVFSIVGALCYA
description Helical; Signal-anchor for type II membrane protein => ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI2
6) chain A
residue 127-147
type TRANSMEM
sequence LPAFLKLWIELLIIRPSSQYI
description Helical; Signal-anchor for type II membrane protein => ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI2
7) chain A
residue 170-190
type TRANSMEM
sequence AAKLVACLCVLLLTAVNCYSV
description Helical; Signal-anchor for type II membrane protein => ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI2
8) chain A
residue 193-214
type TRANSMEM
sequence ATRVQDAFAAAKLLALALIILL
description Helical; Signal-anchor for type II membrane protein => ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI2
9) chain A
residue 243-263
type TRANSMEM
sequence IVLALYSGLFAYGGWNYLNFV
description Helical; Signal-anchor for type II membrane protein => ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI2
10) chain A
residue 277-297
type TRANSMEM
sequence AIIISLPIVTLVYVLTNLAYF
description Helical; Signal-anchor for type II membrane protein => ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI2
11) chain A
residue 325-345
type TRANSMEM
sequence WIIPVFVGLSCFGSVNGSLFT
description Helical; Signal-anchor for type II membrane protein => ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI2
12) chain A
residue 370-390
type TRANSMEM
sequence LLTPVPSLVFTCVMTLLYAFS
description Helical; Signal-anchor for type II membrane protein => ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI2
13) chain D
residue 198-204
type prosite
sequence YTCEATH
description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
source prosite : PS00290
14) chain B
residue 206-630
type TOPO_DOM
sequence RAPRCRELPAQKWWHTGALYRIGDLQAFQGHGAGNLAGLK
GRLDYLSSLKVKGLVLGPIHKNQKDDVAQTDLLQIDPNFG
SKEDFDSLLQSAKKKSIRVILDLTPNYRGENSWFSTQVDT
VATKVKDALEFWLQAGVDGFQVRDIENLKDASSFLAEWQN
ITKGFSEDRLLIAGTNSSDLQQILSLLESNKDLLLTSSYL
SDSGSTGEHTKSLVTQYLNATGNRWCSWSLSQARLLTSFL
PAQLLRLYQLMLFTLPGTPVFSYGDEIGLDAAALPGQPME
APVMLWDESSFPDIPGAVSANMTVKGQSEDPGSLLSLFRR
LSDQRSKERSLLHGDFHAFSAGPGLFSYIRHWDQNERFLV
VLNFGDVGLSAGLQASDLPASASLPAKADLLLSTQPGREE
GSPLELERLKLEPHEGLLLRFPYAA
description Extracellular => ECO:0000269|PubMed:11121428, ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI3
15) chain A
residue 148-169
type TOPO_DOM
sequence VALVFATYLLKPLFPTCPVPEE
description Extracellular => ECO:0000269|PubMed:11121428, ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI3
16) chain A
residue 215-242
type TOPO_DOM
sequence GFVQIFSFEGTKLDVGN
description Extracellular => ECO:0000269|PubMed:11121428, ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI3
17) chain A
residue 298-324
type TOPO_DOM
sequence TTLSTEQMLSSEAVAVDFGNYHLGVMS
description Extracellular => ECO:0000269|PubMed:11121428, ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI3
18) chain A
residue 391-395
type TOPO_DOM
sequence KDIFS
description Extracellular => ECO:0000269|PubMed:11121428, ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI3
19) chain A
residue 452-457
type TOPO_DOM
sequence WKTPVE
description Extracellular => ECO:0000269|PubMed:11121428, ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI3
20) chain B
residue 406
type MOD_RES
sequence S
description Phosphoserine => ECO:0000305|PubMed:19065266
source Swiss-Prot : SWS_FT_FI7
21) chain B
residue 408
type MOD_RES
sequence S
description Phosphoserine => ECO:0000305|PubMed:19065266
source Swiss-Prot : SWS_FT_FI7
22) chain B
residue 410
type MOD_RES
sequence S
description Phosphoserine => ECO:0000305|PubMed:19065266
source Swiss-Prot : SWS_FT_FI7
23) chain B
residue 527
type MOD_RES
sequence S
description Phosphoserine => ECO:0000305|PubMed:19065266
source Swiss-Prot : SWS_FT_FI7
24) chain B
residue 531
type MOD_RES
sequence S
description Phosphoserine => ECO:0000305|PubMed:19065266
source Swiss-Prot : SWS_FT_FI7
25) chain B
residue 424
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:30867591, ECO:0000269|PubMed:33298890, ECO:0000269|PubMed:33758168, ECO:0000269|PubMed:34880232, ECO:0000269|PubMed:35352032, ECO:0007744|PDB:6IRS, ECO:0007744|PDB:7CMI, ECO:0007744|PDB:7DSK, ECO:0007744|PDB:7EPZ, ECO:0007744|PDB:7P9V
source Swiss-Prot : SWS_FT_FI10
26) chain B
residue 506
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:30867591, ECO:0000269|PubMed:33298890, ECO:0000269|PubMed:33758168, ECO:0000269|PubMed:34880232, ECO:0000269|PubMed:35352032, ECO:0007744|PDB:6IRS, ECO:0007744|PDB:7CMH, ECO:0007744|PDB:7DSK, ECO:0007744|PDB:7EPZ, ECO:0007744|PDB:7P9V
source Swiss-Prot : SWS_FT_FI11
27) chain A
residue 105-126
type TOPO_DOM
sequence ELGTTISKSGGDYAYMLEVYGS
description Cytoplasmic => ECO:0000269|PubMed:11121428, ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI1
28) chain A
residue 191-192
type TOPO_DOM
sequence KA
description Cytoplasmic => ECO:0000269|PubMed:11121428, ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI1
29) chain A
residue 264-276
type TOPO_DOM
sequence TEEMINPYRNLPL
description Cytoplasmic => ECO:0000269|PubMed:11121428, ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI1
30) chain A
residue 417-430
type TOPO_DOM
sequence WLRHRKPELERPIK
description Cytoplasmic => ECO:0000269|PubMed:11121428, ECO:0000269|PubMed:30867591
source Swiss-Prot : SWS_FT_FI1
31) chain B
residue 365
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:30867591, ECO:0000269|PubMed:33298890, ECO:0000269|PubMed:33758168, ECO:0000269|PubMed:34880232, ECO:0000269|PubMed:35352032, ECO:0007744|PDB:6IRS, ECO:0007744|PDB:7CMI, ECO:0007744|PDB:7DSK, ECO:0007744|PDB:7EPZ, ECO:0007744|PDB:7P9V
source Swiss-Prot : SWS_FT_FI8
32) chain B
residue 381
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:30867591, ECO:0000269|PubMed:33298890, ECO:0000269|PubMed:33758168, ECO:0000269|PubMed:34880232, ECO:0000269|PubMed:35352032, ECO:0007744|PDB:6IRS, ECO:0007744|PDB:7CMI, ECO:0007744|PDB:7DSK, ECO:0007744|PDB:7EPZ, ECO:0007744|PDB:7P9V
source Swiss-Prot : SWS_FT_FI9

Display surface

Download
Links