eF-site ID 5is0-E
PDB Code 5is0
Chain E

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Title Structure of TRPV1 in complex with capsazepine, determined in lipid nanodisc
Classification TRANSPORT PROTEIN
Compound Transient receptor potential cation channel subfamily V member 1
Source (TRPV1_RAT)
Sequence E:  TPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAY
GPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLL
VEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYY
RPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQ
YFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQR
KEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMIL
RDLCRFMFVYLVFLFGFSTAVVTLIEDGKYNSLYSTCLEL
FKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNM
LIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMR
KAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTT
Description


Functional site

1) chain E
residue 669
type
sequence L
description binding site for residue 6ET B 801
source : AC2

2) chain E
residue 511
type
sequence Y
description binding site for residue 6ET E 801
source : AC4

3) chain E
residue 512
type
sequence S
description binding site for residue 6ET E 801
source : AC4

4) chain E
residue 515
type
sequence L
description binding site for residue 6ET E 801
source : AC4

5) chain E
residue 543
type
sequence F
description binding site for residue 6ET E 801
source : AC4

6) chain E
residue 550
type
sequence T
description binding site for residue 6ET E 801
source : AC4

7) chain E
residue 551
type
sequence N
description binding site for residue 6ET E 801
source : AC4

8) chain E
residue 553
type
sequence L
description binding site for residue 6ET E 801
source : AC4

9) chain E
residue 570
type
sequence E
description binding site for residue 6ET E 801
source : AC4

10) chain E
residue 433-453
type TRANSMEM
sequence IFYFNFFVYCLYMIIFTAAAY
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

11) chain E
residue 472-497
type TRANSMEM
sequence YFRVTGEILSVSGGVYFFFRGIQYFL
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

12) chain E
residue 511-531
type TRANSMEM
sequence YSEILFFVQSLFMLVSVVLYF
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

13) chain E
residue 536-556
type TRANSMEM
sequence EYVASMVFSLAMGWTNMLYYT
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

14) chain E
residue 572-599
type TRANSMEM
sequence MILRDLCRFMFVYLVFLFGFSTAVVTLI
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

15) chain E
residue 658-686
type TRANSMEM
sequence VFIILLLAYVILTYILLLNMLIALMGETV
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

16) chain E
residue 370
type MOD_RES
sequence T
description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871
source Swiss-Prot : SWS_FT_FI10

17) chain E
residue 502
type MOD_RES
sequence S
description Phosphoserine; by PKC/PRKCE => ECO:0000269|PubMed:11884385, ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:14630912
source Swiss-Prot : SWS_FT_FI11

18) chain E
residue 704
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:14630912
source Swiss-Prot : SWS_FT_FI12

19) chain E
residue 627
type CARBOHYD
sequence Y
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872
source Swiss-Prot : SWS_FT_FI13

20) chain E
residue 454-471
type TOPO_DOM
sequence YRPVEGLPPYKLKNTVGD
description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI2

21) chain E
residue 532-535
type TOPO_DOM
sequence SQRK
description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI2

22) chain E
residue 600-649
type TOPO_DOM
sequence EDGKYNSLYSTCLELFKFTIGMGDLEF
description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI2

23) chain E
residue 498-510
type TOPO_DOM
sequence QRRPSLKSLFVDS
description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI3

24) chain E
residue 557-571
type TOPO_DOM
sequence RGFQQMGIYAVMIEK
description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI3

25) chain E
residue 627-649
type INTRAMEM
sequence YNSLYSTCLELFKFTIGMGDLEF
description Pore-forming => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0000305|PubMed:10931826
source Swiss-Prot : SWS_FT_FI4

26) chain E
residue 511
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
source Swiss-Prot : SWS_FT_FI7

27) chain E
residue 550
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
source Swiss-Prot : SWS_FT_FI7

28) chain E
residue 557
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
source Swiss-Prot : SWS_FT_FI7

29) chain E
residue 646
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q9R186
source Swiss-Prot : SWS_FT_FI8


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