eF-site ID 5irz-C
PDB Code 5irz
Chain C

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


Functional site

1) chain C
residue 589
type
sequence F
description binding site for residue 6OE E 804
source : AD1

2) chain C
residue 629
type
sequence S
description binding site for residue 6OE E 804
source : AD1

3) chain C
residue 657
type
sequence A
description binding site for residue 6OE E 806
source : AD3

4) chain C
residue 509
type
sequence D
description binding site for residue 6ES C 802
source : AD9

5) chain C
residue 510
type
sequence S
description binding site for residue 6ES C 802
source : AD9

6) chain C
residue 511
type
sequence Y
description binding site for residue 6ES C 802
source : AD9

7) chain C
residue 512
type
sequence S
description binding site for residue 6ES C 802
source : AD9

8) chain C
residue 550
type
sequence T
description binding site for residue 6ES C 802
source : AD9

9) chain C
residue 557
type
sequence R
description binding site for residue 6ES C 802
source : AD9

10) chain C
residue 570
type
sequence E
description binding site for residue 6ES C 802
source : AD9

11) chain C
residue 699
type
sequence L
description binding site for residue 6ES C 802
source : AD9

12) chain C
residue 700
type
sequence Q
description binding site for residue 6ES C 802
source : AD9

13) chain C
residue 453
type
sequence Y
description binding site for residue 6OE C 803
source : AE1

14) chain C
residue 454
type
sequence Y
description binding site for residue 6OE C 803
source : AE1

15) chain C
residue 454
type
sequence Y
description binding site for residue 6OE C 804
source : AE2

16) chain C
residue 470
type
sequence G
description binding site for residue 6OE C 804
source : AE2

17) chain C
residue 473
type
sequence F
description binding site for residue 6OE C 804
source : AE2

18) chain C
residue 474
type
sequence R
description binding site for residue 6OE C 804
source : AE2

19) chain C
residue 631
type
sequence Y
description binding site for residue 6OE C 805
source : AE3

20) chain C
residue 655
type
sequence F
description binding site for residue 6OE C 806
source : AE4

21) chain C
residue 437
type
sequence N
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

22) chain C
residue 440
type
sequence V
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

23) chain C
residue 488
type
sequence F
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

24) chain C
residue 491
type
sequence R
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

25) chain C
residue 512
type
sequence S
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

26) chain C
residue 513
type
sequence E
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

27) chain C
residue 514
type
sequence I
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

28) chain C
residue 515
type
sequence L
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

29) chain C
residue 517
type
sequence F
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

30) chain C
residue 518
type
sequence V
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

31) chain C
residue 520
type
sequence S
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

32) chain C
residue 551
type
sequence N
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

33) chain C
residue 554
type
sequence Y
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

34) chain C
residue 555
type
sequence Y
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

35) chain C
residue 437
type
sequence N
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

36) chain C
residue 440
type
sequence V
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

37) chain C
residue 487
type
sequence Y
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

38) chain C
residue 488
type
sequence F
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

39) chain C
residue 489
type
sequence F
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

40) chain C
residue 490
type
sequence F
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

41) chain C
residue 492
type
sequence G
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

42) chain C
residue 493
type
sequence I
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

43) chain C
residue 494
type
sequence Q
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

44) chain C
residue 495
type
sequence Y
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

45) chain C
residue 513
type
sequence E
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

46) chain C
residue 516
type
sequence F
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

47) chain C
residue 554
type
sequence Y
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

48) chain C
residue 555
type
sequence Y
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

49) 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

50) 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

51) 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

52) 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

53) 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

54) 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

55) 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

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

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

58) 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

59) 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

60) 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

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

62) 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

63) chain C
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

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

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

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

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

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


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