› 2q7m

X-ray diffraction
4.25Å resolution

Crystal structure of human FLAP with MK-591

Released:
DOI: 10.2210/pdb2q7m/pdb
PDB 2q7m coloured by chain and viewed from the front.
PDB 2q7m coloured by chain and viewed from the side.
PDB 2q7m coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Crystal structure of inhibitor-bound human 5-lipoxygenase-activating protein.
Ferguson AD, McKeever BM, Xu S, Wisniewski D, Miller DK, Yamin TT, Spencer RH, Chu L, Ujjainwalla F, Cunningham BR, Evans JF, Becker JW
Science 317 510-2 (2007)
PMID: 17600184

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arachidonate 5-lipoxygenase-activating protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 161 amino acids
Theoretical weight: 18.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P20292 (Residues: 1-161; Coverage: 100%)
Gene names: ALOX5AP, FLAP
Sequence domains: MAPEG family

Ligands and Environments

1 bound ligand:
Ligand 2CS 6 x 2CS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P4212
Unit cell:
a: 180.6Å b: 180.6Å c: 140.57Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.244 0.242 0.284
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

26 review citations

Untangling the web of 5-lipoxygenase-derived products from a molecular and structural perspective: The battle between pro- and anti-inflammatory lipid mediators.
Gilbert et al. (2021)
25 more

21 mentions without citation

Helical membrane protein conformations and their environment.
Cross et al. (2013)
20 more