› 3v2y

X-ray diffraction
2.8Å resolution

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

Released:
DOI: 10.2210/pdb3v2y/pdb
PDB entry 3v2y coloured by chain, front view.
PDB entry 3v2y coloured by chain, side view.
PDB entry 3v2y coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structure of a lipid G protein-coupled receptor.
Hanson MA, Roth CB, Jo E, Griffith MT, Scott FL, Reinhart G, Desale H, Clemons B, Cahalan SM, Schuerer SC, Sanna MG, Han GW, Kuhn P, Rosen H, Stevens RC
Science 335 851-5 (2012)
PMID: 22344443

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132966 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin; Sphingosine 1-phosphate receptor 1 Chain: A
Molecule details ›
Chain: A
Length: 520 amino acids
Theoretical weight: 58.97 KDa
Source organisms: Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P21453 (Residues: 2-231, 244-326; Coverage: 82%)
  • Canonical: P00720 (Residues: 2-161; Coverage: 98%)
Gene names: CHEDG1, E, EDG1, S1PR1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ML5 1 x ML5
Ligand NAG 1 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P21212
Unit cell:
a: 107.94Å b: 69.7Å c: 81.93Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.229 0.272
Expression system: Spodoptera frugiperda

Quick links

Citations

120 review citations

Molecular signatures of G-protein-coupled receptors.
Venkatakrishnan et al. (2013)
119 more

108 mentions without citation

Generic GPCR residue numbers - aligning topology maps while minding the gaps.
Isberg et al. (2015)
107 more