3V2W
Crystal Structure of a Lipid G protein-Coupled Receptor at 3.35A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003796 | molecular_function | lysozyme activity |
A | 0004930 | molecular_function | G protein-coupled receptor activity |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0009253 | biological_process | peptidoglycan catabolic process |
A | 0016020 | cellular_component | membrane |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0016998 | biological_process | cell wall macromolecule catabolic process |
A | 0030430 | cellular_component | host cell cytoplasm |
A | 0031640 | biological_process | killing of cells of another organism |
A | 0042742 | biological_process | defense response to bacterium |
A | 0044659 | biological_process | viral release from host cell by cytolysis |
Functional Information from PROSITE/UniProt
site_id | PS00237 |
Number of Residues | 17 |
Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASVfSLLAIAIERYItM |
Chain | Residue | Details |
A | ALA130-MET146 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=1 |
Chain | Residue | Details |
A | LEU47-LEU68 |
site_id | SWS_FT_FI2 |
Number of Residues | 34 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:15750791 |
Chain | Residue | Details |
A | THR69-TYR82 | |
A | ALA139-LEU160 |
site_id | SWS_FT_FI3 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=2 |
Chain | Residue | Details |
A | PHE83-LEU104 |
site_id | SWS_FT_FI4 |
Number of Residues | 34 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:15750791 |
Chain | Residue | Details |
A | SER105-GLN116 | |
A | ASN183-PRO196 | |
A | VAL280-LEU290 |
site_id | SWS_FT_FI5 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=3 |
Chain | Residue | Details |
A | TRP117-ILE138 |
site_id | SWS_FT_FI6 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=4 |
Chain | Residue | Details |
A | PHE161-TRP182 |
site_id | SWS_FT_FI7 |
Number of Residues | 27 |
Details | TRANSMEM: Helical; Name=5 |
Chain | Residue | Details |
A | LEU197-ILE224 |
site_id | SWS_FT_FI8 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=6 |
Chain | Residue | Details |
A | ILE259-ASP279 |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=7 |
Chain | Residue | Details |
A | PHE291-TYR311 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | ARG120 | |
A | ILE266 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O08530 |
Chain | Residue | Details |
A | LYS10 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15750791, ECO:0000269|PubMed:22344443 |
Chain | Residue | Details |
A | ASN30 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN36 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | GLU1011 |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | ACT_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 |
Chain | Residue | Details |
A | ASP1020 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | LEU1032 | |
A | PHE1104 |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000303|PubMed:7831309 |
Chain | Residue | Details |
A | SER1117 | |
A | ASN1132 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 921 |
Chain | Residue | Details |
A | GLU1011 | proton shuttle (general acid/base) |
A | ASP1020 | covalent catalysis |