› 6lw5

X-ray diffraction
2.8Å resolution

Crystal structure of the human formyl peptide receptor 2 in complex with WKYMVm

Released:
DOI: 10.2210/pdb6lw5/pdb
PDB entry 6lw5 coloured by chain, front view.
PDB entry 6lw5 coloured by chain, side view.
PDB entry 6lw5 coloured by chain, top view.
Source organisms:
Primary publication:
Structural basis of ligand binding modes at the human formyl peptide receptor 2.
Chen T, Xiong M, Zong X, Ge Y, Zhang H, Wang M, Won Han G, Yi C, Ma L, Ye RD, Xu Y, Zhao Q, Wu B
Nat Commun 11 1208 (2020)
PMID: 32139677

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142052 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
N-formyl peptide receptor 2; Soluble cytochrome b562 Chain: A
Molecule details ›
Chain: A
Length: 427 amino acids
Theoretical weight: 47.69 KDa
Source organisms: Expression system: Mammalian expression vector Flag-MCS-pcDNA3.1
UniProt:
  • Canonical: P0ABE7 (Residues: 23-128; Coverage: 100%)
  • Canonical: P25090 (Residues: 3-322; Coverage: 91%)
Gene names: FPR2, FPRH1, FPRL1, LXA4R, cybC
Sequence domains:
TRP-LYS-TYR-MET-VAL-QXV Chain: B
Molecule details ›
Chain: B
Length: 6 amino acids
Theoretical weight: 857 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand CLR 2 x CLR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P3221
Unit cell:
a: 66.28Å b: 66.28Å c: 244.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.258 0.258 0.289
Expression systems:
  • Mammalian expression vector Flag-MCS-pcDNA3.1
  • Not provided

Quick links

Citations

8 review citations

Formyl peptide receptor type 2 agonists to kick-start resolution pharmacology.
Perretti et al. (2020)
7 more

13 mentions without citation

G protein-coupled receptors: structure- and function-based drug discovery.
Yang et al. (2021)
12 more