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6LN2

Crystal structure of full length human GLP1 receptor in complex with Fab fragment (Fab7F38)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004888molecular_functiontransmembrane signaling receptor activity
A0004930molecular_functionG protein-coupled receptor activity
A0004967molecular_functionglucagon receptor activity
A0005506molecular_functioniron ion binding
A0007166biological_processcell surface receptor signaling pathway
A0007186biological_processG protein-coupled receptor signaling pathway
A0008528molecular_functionG protein-coupled peptide receptor activity
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0043448biological_processalkane catabolic process
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00202
Number of Residues11
DetailsRUBREDOXIN Rubredoxin signature. IpDDWvCPlCG
ChainResidueDetails
AILE1033-GLY1043

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCNVDH
ChainResidueDetails
CTYR206-HIS212
BTYR191-HIS197

site_idPS00649
Number of Residues25
DetailsG_PROTEIN_RECEP_F2_1 G-protein coupled receptors family 2 signature 1. CnrtFDeya.CWpdGepgsfvnvsCP
ChainResidueDetails
ACYS62-PRO86

site_idPS00650
Number of Residues16
DetailsG_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGLMVaILYCFvNneV
ChainResidueDetails
AGLN394-VAL409

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues166
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:28514449
ChainResidueDetails
AARG24-GLU139
ALYS202-ARG227
ATYR291-TYR305
AMET371-LYS383

site_idSWS_FT_FI2
Number of Residues24
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:28514449
ChainResidueDetails
AGLN140-ALA164

site_idSWS_FT_FI3
Number of Residues29
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:28514449
ChainResidueDetails
AILE165-THR175
ACYS329-ARG348

site_idSWS_FT_FI4
Number of Residues25
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:28514449
ChainResidueDetails
AARG176-LEU201

site_idSWS_FT_FI5
Number of Residues23
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:28514449
ChainResidueDetails
ALEU228-LEU251

site_idSWS_FT_FI6
Number of Residues24
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:28514449
ChainResidueDetails
APHE266-LEU290

site_idSWS_FT_FI7
Number of Residues22
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:28514449
ChainResidueDetails
ATRP306-ILE328

site_idSWS_FT_FI8
Number of Residues21
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:28514449
ChainResidueDetails
ALEU349-VAL370

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:28514449
ChainResidueDetails
ALEU384-PHE404

site_idSWS_FT_FI10
Number of Residues2
DetailsSITE: Interaction with the endogenous ligand GLP-1 => ECO:0000269|PubMed:19861722
ChainResidueDetails
AARG121
AGLU128

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: ADP-ribosylcysteine => ECO:0000269|PubMed:21901419
ChainResidueDetails
ACYS341

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: ADP-ribosylarginine => ECO:0000269|PubMed:21901419
ChainResidueDetails
AARG348

site_idSWS_FT_FI13
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22412906
ChainResidueDetails
AASN63
AASN82
AASN115

site_idSWS_FT_FI14
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00241, ECO:0000269|PubMed:10216292
ChainResidueDetails
ACYS1006
ACYS1009
ACYS1039
ACYS1042

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: N-formylmethionine => ECO:0000269|PubMed:1637309
ChainResidueDetails
AMET1001

226707

PDB entries from 2024-10-30

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