Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3V2Y

Crystal Structure of a Lipid G protein-Coupled Receptor at 2.80A

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0008152biological_processmetabolic process
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASVfSLLAIAIERYItM
ChainResidueDetails
AALA130-MET146

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
ALEU47-LEU68

site_idSWS_FT_FI2
Number of Residues34
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:15750791
ChainResidueDetails
ATHR69-TYR82
AALA139-LEU160

site_idSWS_FT_FI3
Number of Residues21
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
APHE83-LEU104

site_idSWS_FT_FI4
Number of Residues34
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:15750791
ChainResidueDetails
ASER105-GLN116
AASN183-PRO196
AVAL280-LEU290

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
ATRP117-ILE138

site_idSWS_FT_FI6
Number of Residues21
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
APHE161-TRP182

site_idSWS_FT_FI7
Number of Residues27
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
ALEU197-ILE224

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
AILE259-ASP279

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
APHE291-TYR311

site_idSWS_FT_FI10
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AARG120
AILE266

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O08530
ChainResidueDetails
ALYS10

site_idSWS_FT_FI12
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15750791, ECO:0000269|PubMed:22344443
ChainResidueDetails
AASN30

site_idSWS_FT_FI13
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN36

site_idSWS_FT_FI14
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU1011

site_idSWS_FT_FI15
Number of Residues1
DetailsACT_SITE: 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
ChainResidueDetails
AASP1020

site_idSWS_FT_FI16
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU1032
APHE1104

site_idSWS_FT_FI17
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER1117
AASN1132

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU1011proton shuttle (general acid/base)
AASP1020covalent catalysis

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon