eF-site/Summary 5dgy-B

eF-site ID	5dgy-B
PDB Code	5dgy
Chain	B

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Title	Crystal structure of rhodopsin bound to visual arrestin
Classification	SIGNALING PROTEIN
Compound	Endolysin,Rhodopsin,S-arrestin
Source	(ARRS_MOUSE)

Sequence	B:	MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSML AAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLA VADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLQGFFATLG GEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFT WVMALACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNN ESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQES ATTQKAEKEVTRMVIIYVIAFLICWVPYASVAFYIFTHQG SCFGPIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTT ICCGKNVIFKKVSRDKSVTIYLGKRDYVDHVSQVEPVDGV VLVDPELVKGKKVYVTLTCAFRYGQEDIDVMGLTFRRDLY FSRVQVYPPVGAMSVLTQLQESLLKKLGDNTYPFLLTFPD YLPCSVMLQPAPQDVGKSCGVDFEVKAFASDITDPEEDKI PKKSSVRLLIRKVQHAPPEMGPQPSAEASWQFFMSDKPLN LSVSLSKEIYFHGEPIPVTVTVTNNTDKVVKKIKVSVEQI ANVVLYSSDYYVKPVASEETQEKVQPNSTLTKTLVLVPLL ANNRERRGIALDGKIKHEDTNLASSTIIKEGIDRTVMGIL VSYHIKVKLTVSGFLTSSEVATEVPFRLMHPQP

Description

Functional site


1)	chain	B
	residue	322
	type	LIPID
	sequence	C
	description	S-palmitoyl cysteine => ECO:0000250\|UniProtKB:P02699
	source	Swiss-Prot : SWS_FT_FI22

2)	chain	B
	residue	323
	type	LIPID
	sequence	C
	description	S-palmitoyl cysteine => ECO:0000250\|UniProtKB:P02699
	source	Swiss-Prot : SWS_FT_FI22

3)	chain	B
	residue	2
	type	CARBOHYD
	sequence	C
	description	N-linked (GlcNAc...) asparagine => ECO:0000250\|UniProtKB:P02699
	source	Swiss-Prot : SWS_FT_FI23

4)	chain	B
	residue	15
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:28753425
	source	Swiss-Prot : SWS_FT_FI24

5)	chain	B
	residue	1231
	type	MOD_RES
	sequence	T
	description	Phosphothreonine => ECO:0000250\|UniProtKB:P15887
	source	Swiss-Prot : SWS_FT_FI25

6)	chain	B
	residue	1-36
	type	TOPO_DOM
	sequence	MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQ
	description	Extracellular => ECO:0000269\|PubMed:26200343, ECO:0000269\|PubMed:28753425
	source	Swiss-Prot : SWS_FT_FI5

7)	chain	B
	residue	97-110
	type	TOPO_DOM
	sequence	TSLHGYFVFGPTGC
	description	Extracellular => ECO:0000269\|PubMed:26200343, ECO:0000269\|PubMed:28753425
	source	Swiss-Prot : SWS_FT_FI5

8)	chain	B
	residue	174-202
	type	TOPO_DOM
	sequence	GWSRYIPEGLQCSCGIDYYTLKPEVNNES
	description	Extracellular => ECO:0000269\|PubMed:26200343, ECO:0000269\|PubMed:28753425
	source	Swiss-Prot : SWS_FT_FI5

9)	chain	B
	residue	275-284
	type	TOPO_DOM
	sequence	IFTHQGSCFG
	description	Extracellular => ECO:0000269\|PubMed:26200343, ECO:0000269\|PubMed:28753425
	source	Swiss-Prot : SWS_FT_FI5

10)	chain	B
	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

11)	chain	B
	residue	62-73
	type	TOPO_DOM
	sequence	TVQHKKLRTPLN
	description	Cytoplasmic => ECO:0000269\|PubMed:26200343, ECO:0000269\|PubMed:28753425
	source	Swiss-Prot : SWS_FT_FI7

12)	chain	B
	residue	134-152
	type	TOPO_DOM
	sequence	ERYVVVCKPMSNFRFGENH
	description	Cytoplasmic => ECO:0000269\|PubMed:26200343, ECO:0000269\|PubMed:28753425
	source	Swiss-Prot : SWS_FT_FI7

13)	chain	B
	residue	225-252
	type	TOPO_DOM
	sequence	QLVFTVKEAAAQQQESATTQKAEKEVTR
	description	Cytoplasmic => ECO:0000269\|PubMed:26200343, ECO:0000269\|PubMed:28753425
	source	Swiss-Prot : SWS_FT_FI7

14)	chain	B
	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

15)	chain	B
	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

16)	chain	B
	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

17)	chain	B
	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

18)	chain	B
	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

19)	chain	B
	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

20)	chain	B
	residue	201
	type	BINDING
	sequence	E
	description	BINDING => ECO:0000250\|UniProtKB:P02699
	source	Swiss-Prot : SWS_FT_FI14

21)	chain	B
	residue	279
	type	BINDING
	sequence	Q
	description	BINDING => ECO:0000250\|UniProtKB:P02699
	source	Swiss-Prot : SWS_FT_FI14

22)	chain	B
	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

23)	chain	B
	residue	1
	type	MOD_RES
	sequence	M
	description	N-acetylmethionine => ECO:0000250\|UniProtKB:P02699
	source	Swiss-Prot : SWS_FT_FI16

24)	chain	B
	residue	296
	type	MOD_RES
	sequence	K
	description	N6-(retinylidene)lysine => ECO:0000250\|UniProtKB:P02699
	source	Swiss-Prot : SWS_FT_FI17