eF-site ID 3j5r-C
PDB Code 3j5r
Chain C

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Title Reconstruction of TRPV1 ion channel in complex with capsaicin by single particle cryo-microscopy
Classification TRANSPORT PROTEIN
Compound Transient receptor potential cation channel subfamily V member 1
Source (3J5R)
Sequence C:  LYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKD
PETGKTCLLKAMLNLHNGQNDTIALLLDVARKTDSLKQFV
NASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAA
ANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQN
SWQPADISARDSVGNTVLHALVEVADNTVDNTKFVTSMYN
EILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLA
YILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTC
EKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFV
KRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVG
DYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSVDSYSEIL
FFVQSLFMLVSVVLYFSQRKEYVASMVFSLAMGWTNMLYY
TRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAV
VTLIEDGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAV
FIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWK
LQRAITILDTEKSFLKCMRKAXXXXXXXXXXX
Description


Functional site
1) chain C
residue 433-453
type TRANSMEM
sequence IFYFNFFVYCLYMIIFTAAAY
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1
2) chain C
residue 472-497
type TRANSMEM
sequence YFRVTGEILSVSGGVYFFFRGIQYFL
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1
3) chain C
residue 511-531
type TRANSMEM
sequence YSEILFFVQSLFMLVSVVLYF
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1
4) chain C
residue 536-556
type TRANSMEM
sequence EYVASMVFSLAMGWTNMLYYT
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1
5) chain C
residue 572-599
type TRANSMEM
sequence MILRDLCRFMFVYLVFLFGFSTAVVTLI
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1
6) chain C
residue 681-709
type TRANSMEM
sequence LMGETVNKIAQESKNIWKLQRAITILDTE
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1
7) chain C
residue 454-471
type TOPO_DOM
sequence YRPVEGLPPYKLKNTVGD
description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI2
8) chain C
residue 532-535
type TOPO_DOM
sequence SQRK
description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI2
9) chain C
residue 600-649
type TOPO_DOM
sequence EDGKYNSLYSTCLELFKFTIGMGDLEF
description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI2
10) chain C
residue 498-510
type TOPO_DOM
sequence QRRPSVDS
description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI3
11) chain C
residue 557-571
type TOPO_DOM
sequence RGFQQMGIYAVMIEK
description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI3
12) chain C
residue 650-672
type INTRAMEM
sequence TENYDFKAVFIILLLAYVILTYI
description Pore-forming => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0000305|PubMed:10931826
source Swiss-Prot : SWS_FT_FI4
13) chain C
residue 115
type BINDING
sequence R
description BINDING => ECO:0007744|PDB:2PNN
source Swiss-Prot : SWS_FT_FI5
14) chain C
residue 155
type BINDING
sequence K
description BINDING => ECO:0007744|PDB:2PNN
source Swiss-Prot : SWS_FT_FI5
15) chain C
residue 210
type BINDING
sequence E
description BINDING => ECO:0007744|PDB:2PNN
source Swiss-Prot : SWS_FT_FI5
16) chain C
residue 160
type BINDING
sequence K
description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN
source Swiss-Prot : SWS_FT_FI6
17) chain C
residue 164
type BINDING
sequence N
description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN
source Swiss-Prot : SWS_FT_FI6
18) chain C
residue 199
type BINDING
sequence Y
description BINDING => ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN
source Swiss-Prot : SWS_FT_FI6
19) chain C
residue 511
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
source Swiss-Prot : SWS_FT_FI7
20) chain C
residue 550
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
source Swiss-Prot : SWS_FT_FI7
21) chain C
residue 557
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
source Swiss-Prot : SWS_FT_FI7
22) chain C
residue 669
type BINDING
sequence L
description BINDING => ECO:0000250|UniProtKB:Q9R186
source Swiss-Prot : SWS_FT_FI8
23) chain C
residue 116
type MOD_RES
sequence S
description Phosphoserine; by PKA and PKD => ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:15471852
source Swiss-Prot : SWS_FT_FI9
24) chain C
residue 144
type MOD_RES
sequence T
description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871
source Swiss-Prot : SWS_FT_FI10
25) chain C
residue 370
type MOD_RES
sequence T
description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871
source Swiss-Prot : SWS_FT_FI10
26) chain C
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
27) chain C
residue 758
type MOD_RES
sequence X
description Phosphothreonine => ECO:0000269|PubMed:14630912
source Swiss-Prot : SWS_FT_FI12
28) chain C
residue 627
type CARBOHYD
sequence Y
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872
source Swiss-Prot : SWS_FT_FI13

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