eF-site ID 4zwj-C
PDB Code 4zwj
Chain C

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Title Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser
Classification SIGNALING PROTEIN
Compound Chimera protein of human Rhodopsin, mouse S-arrestin, and T4 Endolysin
Source Mus musculus (Mouse) (ARRS_MOUSE)
Sequence C:  NIFEMLRIDEGVITKDEAEKLFNQDVDAAVRGILRNAKLK
PVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKR
WDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYMCGT
EGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSMLAAYM
FLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADL
FMVLGGFTSTLYTSLHGYFVFGPTGCNLQGFFATLGGEIA
LWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMA
LACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNNESFV
IYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQESATTQ
KAEKEVTRMVIIYVIAFLICWVPYASVAFYIFTHQGSCFG
PIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTTICCG
KNVIFKKVSRDKSVTIYLGKRDYVDHVSQVEPVDGVVLVD
PELVKGKKVYVTLTCAFRYGQEDIDVMGLTFRRDLYFSRV
QVYPPVGAMSVLTQLQESLLKKLGDNTYPFLLTFPDYLPC
SVMLQPAPQDVGKSCGVDFEVKAFASDITDPEEDKIPKKS
SVRLLIRKVQHAPPEMGPQPSAEASWQFFMSDKPLNLSVS
LSKEIYFHGEPIPVTVTVTNNTDKVVKKIKVSVEQIANVV
LYSSDYYVKPVASEETQEKVQPNSTLTKTLVLVPLLANNR
ERRGIALDGKIKHEDTNLASSTIIKEGIDRTVMGILVSYH
IKVKLTVSGFLTSSEVATEVPFRLMHPQP
Description


Functional site
1) chain C
residue 322
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI22
2) chain C
residue 323
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI22
3) chain C
residue 2
type CARBOHYD
sequence C
description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI23
4) chain C
residue 15
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI24
5) chain C
residue 2231
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P15887
source Swiss-Prot : SWS_FT_FI25
6) chain C
residue 1011
type ACT_SITE
sequence E
description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI1
7) chain C
residue 1104
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI3
8) chain C
residue 1117
type BINDING
sequence S
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI4
9) chain C
residue 1132
type BINDING
sequence N
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI4
10) chain C
residue 1-36
type TOPO_DOM
sequence MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQ
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5
11) chain C
residue 97-110
type TOPO_DOM
sequence TSLHGYFVFGPTGC
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5
12) chain C
residue 174-202
type TOPO_DOM
sequence GWSRYIPEGLQCSCGIDYYTLKPEVNNES
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5
13) chain C
residue 275-284
type TOPO_DOM
sequence IFTHQGSCFG
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5
14) chain C
residue 37-61
type TRANSMEM
sequence FSMLAAYMFLLIVLGFPINFLTLYV
description Helical; Name=1 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI6
15) chain C
residue 62-73
type TOPO_DOM
sequence TVQHKKLRTPLN
description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI7
16) chain C
residue 134-152
type TOPO_DOM
sequence ERYVVVCKPMSNFRFGENH
description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI7
17) chain C
residue 225-252
type TOPO_DOM
sequence QLVFTVKEAAAQQQESATTQKAEKEVTR
description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI7
18) chain C
residue 74-96
type TRANSMEM
sequence YILLNLAVADLFMVLGGFTSTLY
description Helical; Name=2 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI8
19) chain C
residue 111-133
type TRANSMEM
sequence NLQGFFATLGGEIALWSLVVLAI
description Helical; Name=3 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI9
20) chain C
residue 153-173
type TRANSMEM
sequence AIMGVAFTWVMALACAAPPLA
description Helical; Name=4 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI10
21) chain C
residue 203-224
type TRANSMEM
sequence FVIYMFVVHFTIPMIIIFFCYG
description Helical; Name=5 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI11
22) chain C
residue 253-274
type TRANSMEM
sequence MVIIYVIAFLICWVPYASVAFY
description Helical; Name=6 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI12
23) chain C
residue 285-309
type TRANSMEM
sequence PIFMTIPAFFAKSAAIYNPVIYIMM
description Helical; Name=7 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI13
24) chain C
residue 201
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI14
25) chain C
residue 279
type BINDING
sequence Q
description BINDING => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI14
26) chain C
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_FI15
27) chain C
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI16
28) chain C
residue 296
type MOD_RES
sequence K
description N6-(retinylidene)lysine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI17
29) chain C
residue 1011
type catalytic
sequence E
description 921
source MCSA : MCSA3

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