eF-site ID 5w0p-D
PDB Code 5w0p
Chain D

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Title Crystal structure of rhodopsin bound to visual arrestin determined by X-ray free electron laser
Classification SIGNALING PROTEIN
Compound Endolysin,Rhodopsin,S-arrestin
Source (ARRS_MOUSE)
Sequence D:  RGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFT
NSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRT
GTWDAYMCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEP
WQFSMLAAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNY
ILLNLAVADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLQG
FFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAI
MGVAFTWVMALACAAPPLAGWSRYIPEGLQCSCGIDYYTL
KPEVNNESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAA
AQQQESATTQKAEKEVTRMVIIYVIAFLICWVPYASVAFY
IFTHQGSCFGPIFMTIPAFFAKSAAIYNPVIYIMMNKQFR
NCMLTTICCGDDEASATVXKTETSVIFKKVSRDKSVTIYL
GKRDYVDHVSQVEPVDGVVLVDPELVKGKKVYVTLTCAFR
YGQEDIDVMGLTFRRDLYFSRVQVYPPVGAMSVLTQLQES
LLKKLGDNTYPFLLTFPDYLPCSVMLQPAPQDVGKSCGVD
FEVKAFASDITDPEEDKIPKKSSVRLLIRKVQHAPPEMGP
QPSAEASWQFFMSDKPLNLSVSLSKEIYFHGEPIPVTVTV
TNNTDKVVKKIKVSVEQIANVVLYSSDYYVKPVASEETQE
KVQPNSTLTKTLVLVPLLANNRERRGIALDGKIKHEDTNL
ASSTIIKEGIDRTVMGILVSYHIKVKLTVSGFLGELTSSE
VATEVPFRLMHPQP
Description


Functional site

1) chain D
residue 1-36
type TOPO_DOM
sequence MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQ
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI1

2) chain D
residue 97-110
type TOPO_DOM
sequence TSLHGYFVFGPTGC
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI1

3) chain D
residue 174-202
type TOPO_DOM
sequence GWSRYIPEGLQCSCGIDYYTLKPEVNNES
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI1

4) chain D
residue 275-284
type TOPO_DOM
sequence IFTHQGSCFG
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI1

5) chain D
residue 201
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI10

6) chain D
residue 279
type BINDING
sequence Q
description BINDING => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI10

7) chain D
residue 113
type SITE
sequence Q
description Plays an important role in the conformation switch to the active conformation => ECO:0000269|PubMed:26200343
source Swiss-Prot : SWS_FT_FI11

8) chain D
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI12

9) chain D
residue 296
type MOD_RES
sequence K
description N6-(retinylidene)lysine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI13

10) chain D
residue 334
type MOD_RES
sequence S
description Phosphoserine => ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI14

11) chain D
residue 338
type MOD_RES
sequence X
description Phosphoserine => ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI14

12) chain D
residue 336
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI15

13) chain D
residue 340
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI16

14) chain D
residue 342
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI16

15) chain D
residue 343
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI17

16) chain D
residue 322
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI18

17) chain D
residue 323
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI18

18) chain D
residue 2
type CARBOHYD
sequence C
description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI19

19) chain D
residue 37-61
type TRANSMEM
sequence FSMLAAYMFLLIVLGFPINFLTLYV
description Helical; Name=1 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI2

20) chain D
residue 15
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI20

21) chain D
residue 2231
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P15887
source Swiss-Prot : SWS_FT_FI21

22) chain D
residue -57
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI24

23) chain D
residue -44
type BINDING
sequence S
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI25

24) chain D
residue -29
type BINDING
sequence N
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI25

25) chain D
residue 62-73
type TOPO_DOM
sequence TVQHKKLRTPLN
description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI3

26) chain D
residue 134-152
type TOPO_DOM
sequence ERYVVVCKPMSNFRFGENH
description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI3

27) chain D
residue 225-252
type TOPO_DOM
sequence QLVFTVKEAAAQQQESATTQKAEKEVTR
description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI3

28) chain D
residue 74-96
type TRANSMEM
sequence YILLNLAVADLFMVLGGFTSTLY
description Helical; Name=2 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI4

29) chain D
residue 111-133
type TRANSMEM
sequence NLQGFFATLGGEIALWSLVVLAI
description Helical; Name=3 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5

30) chain D
residue 153-173
type TRANSMEM
sequence AIMGVAFTWVMALACAAPPLA
description Helical; Name=4 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI6

31) chain D
residue 203-224
type TRANSMEM
sequence FVIYMFVVHFTIPMIIIFFCYG
description Helical; Name=5 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI7

32) chain D
residue 253-274
type TRANSMEM
sequence MVIIYVIAFLICWVPYASVAFY
description Helical; Name=6 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI8

33) chain D
residue 285-309
type TRANSMEM
sequence PIFMTIPAFFAKSAAIYNPVIYIMM
description Helical; Name=7 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI9


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