eF-site ID 5yqz-PR
PDB Code 5yqz
Chain P, R

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Title Structure of the glucagon receptor in complex with a glucagon analogue
Classification SIGNALING PROTEIN/HYDROLASE
Compound Glucagon receptor,Endolysin,Glucagon receptor
Source null (5YQZ)
Sequence P:  SQGTFTSEYSKYLDSRRAQDFVKWLLNT
R:  QVMDFLFEKWKLYGDQCHHNLSLLPPPTELVCNRTFDKYS
CWPDTPANTTANISCPWYLPWHHKVQHRFVFKRCGPDGQW
VRGPRGQPWRDASQCQMDGEEIEVQKEVAKMYSSFQVMYT
VGYSLSLGALLLALAILGGLSKLHCTANAIHANLFASFVL
KASSVLVIDGLLRTRYSQKIGDDLSVSTWLSDGAVAGCRV
AAVFMQYGIVANYCWLLVEGLYLHNLLGLATNIFEMLRID
EGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAI
GRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDS
LDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAA
VNLAKSRWYNQTPNRAKRVITTFRTGTWDAYERSFFSLYL
GIGWGAPMLFVVPWAVVKCLFENVQCWTSNDNMGFWWILR
FPVFLAILINFFIFVRIVQLLVAKLRARQMHHTDYKFRLA
KSTLTLIPLLGVHEVVFAFVTDEHAQGTLRSAKLFFDLFL
SSFQGLLVAVLYCFLNKEVQSELRRRWHRWRLGKVLWE
Description


Functional site

1) chain R
residue 174-198
type TRANSMEM
sequence NAIHANLFASFVLKASSVLVIDGLL
description Helical; Name=2 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451
source Swiss-Prot : SWS_FT_FI3

2) chain R
residue 199-225
type TOPO_DOM
sequence RTRYSQKIGDDLSVSTWLSDGAVAGCR
description Extracellular => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451
source Swiss-Prot : SWS_FT_FI4

3) chain R
residue 286-303
type TOPO_DOM
sequence KCLFENVQCWTSNDNMGF
description Extracellular => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451
source Swiss-Prot : SWS_FT_FI4

4) chain R
residue 370-381
type TOPO_DOM
sequence DEHAQGTLRSAK
description Extracellular => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451
source Swiss-Prot : SWS_FT_FI4

5) chain R
residue 226-249
type TRANSMEM
sequence VAAVFMQYGIVANYCWLLVEGLYL
description Helical; Name=3 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451
source Swiss-Prot : SWS_FT_FI5

6) chain R
residue 264-285
type TRANSMEM
sequence FSLYLGIGWGAPMLFVVPWAVV
description Helical; Name=4 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451
source Swiss-Prot : SWS_FT_FI6

7) chain R
residue 304-326
type TRANSMEM
sequence WWILRFPVFLAILINFFIFVRIV
description Helical; Name=5 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451
source Swiss-Prot : SWS_FT_FI7

8) chain R
residue 351-369
type TRANSMEM
sequence TLTLIPLLGVHEVVFAFVT
description Helical; Name=6 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451
source Swiss-Prot : SWS_FT_FI8

9) chain R
residue 382-402
type TRANSMEM
sequence LFFDLFLSSFQGLLVAVLYCF
description Helical; Name=7 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451
source Swiss-Prot : SWS_FT_FI9

10) chain R
residue 46
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28514451
source Swiss-Prot : SWS_FT_FI10

11) chain R
residue 59
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28514451
source Swiss-Prot : SWS_FT_FI10

12) chain R
residue 74
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22908259, ECO:0000269|PubMed:28514451, ECO:0007744|PDB:4ERS
source Swiss-Prot : SWS_FT_FI11

13) chain R
residue 78
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22908259, ECO:0000269|PubMed:28514451, ECO:0007744|PDB:4ERS
source Swiss-Prot : SWS_FT_FI11

14) chain R
residue 1010
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_FI12

15) chain R
residue 1019
type ACT_SITE
sequence D
description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI13

16) chain R
residue 1031
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI14

17) chain R
residue 1103
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI14

18) chain R
residue 1116
type BINDING
sequence S
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI15

19) chain R
residue 1131
type BINDING
sequence N
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI15

20) chain R
residue 58-82
type prosite
sequence CNRTFDKYSCWPDTPANTTANISCP
description G_PROTEIN_RECEP_F2_1 G-protein coupled receptors family 2 signature 1. CnrtFDkys.CWpdTpanttanisCP
source prosite : PS00649

21) chain R
residue 392-407
type prosite
sequence QGLLVAVLYCFLNKEV
description G_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGLLVaVLYCFlNkeV
source prosite : PS00650

22) chain R
residue 1010
type catalytic
sequence E
description 921
source MCSA : MCSA1

23) chain R
residue 1019
type catalytic
sequence D
description 921
source MCSA : MCSA1

24) chain P
residue 2
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P55095
source Swiss-Prot : SWS_FT_FI1

25) chain R
residue 162-173
type TOPO_DOM
sequence ILGGLSKLHCTA
description Cytoplasmic => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451
source Swiss-Prot : SWS_FT_FI2

26) chain R
residue 327-350
type TOPO_DOM
sequence QLLVAKLRARQMHHTDYKFRLAKS
description Cytoplasmic => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451
source Swiss-Prot : SWS_FT_FI2


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