Bromine in PDB 3qkv: Crystal Structure of Fatty Acid Amide Hydrolase with Small Molecule Compound

All present enzymatic activity of Crystal Structure of Fatty Acid Amide Hydrolase with Small Molecule Compound:
3.5.1.99;

The structure of Crystal Structure of Fatty Acid Amide Hydrolase with Small Molecule Compound, PDB code: 3qkv was solved by X.Min, N.P.C.Walker, Z.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 3.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	90.820, 104.080, 147.850, 90.00, 90.00, 90.00
R / Rfree (%)	26.7 / 28.9

The binding sites of Bromine atom in the Crystal Structure of Fatty Acid Amide Hydrolase with Small Molecule Compound (pdb code 3qkv). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Crystal Structure of Fatty Acid Amide Hydrolase with Small Molecule Compound, PDB code: 3qkv:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Crystal Structure of Fatty Acid Amide Hydrolase with Small Molecule Compound


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Fatty Acid Amide Hydrolase with Small Molecule Compound within 5.0Å range: probe atom residue distance (Å) B Occ B:Br580 b:40.8 occ:1.00 BR1 B:QKV580 0.0 40.8 1.0 C14 B:QKV580 1.9 39.3 1.0 C11 B:QKV580 2.9 38.8 1.0 C15 B:QKV580 2.9 39.0 1.0 CE2 B:PHE381 3.6 29.3 1.0 CZ B:PHE381 3.9 29.3 1.0 CG2 B:THR488 4.0 23.2 1.0 C3 B:QKV580 4.2 38.1 1.0 C13 B:QKV580 4.2 38.4 1.0 SD B:MET436 4.4 34.0 1.0 CE B:MET436 4.4 34.0 1.0 CD1 B:PHE432 4.4 34.6 1.0 CE1 B:PHE432 4.5 34.6 1.0 CD2 B:PHE381 4.5 29.3 1.0 C4 B:QKV580 4.7 38.0 1.0 CE1 B:PHE381 5.0 29.3 1.0

Bromine binding site 2 out of 2 in the Crystal Structure of Fatty Acid Amide Hydrolase with Small Molecule Compound


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of Fatty Acid Amide Hydrolase with Small Molecule Compound within 5.0Å range: probe atom residue distance (Å) B Occ A:Br580 b:40.1 occ:1.00 BR1 A:QKV580 0.0 40.1 1.0 C14 A:QKV580 1.9 38.6 1.0 C11 A:QKV580 2.9 38.2 1.0 C15 A:QKV580 2.9 38.4 1.0 CG2 A:THR488 3.7 25.4 1.0 CE2 A:PHE381 3.7 26.5 1.0 CD1 A:LEU404 3.9 31.1 1.0 CZ A:PHE381 4.1 26.5 1.0 C3 A:QKV580 4.2 37.5 1.0 C13 A:QKV580 4.2 37.8 1.0 CE2 A:PHE432 4.3 32.3 1.0 CD2 A:PHE432 4.4 32.4 1.0 SD A:MET436 4.5 31.6 1.0 C4 A:QKV580 4.7 37.4 1.0 CD2 A:PHE381 4.7 26.6 1.0 CE A:MET436 4.9 31.6 1.0

X.Min, S.T.Thibault, A.C.Porter, D.J.Gustin, T.J.Carlson, H.Xu, M.Lindstrom, G.Xu, C.Uyeda, Z.Ma, Y.Li, F.Kayser, N.P.Walker, Z.Wang. Discovery and Molecular Basis of Potent Noncovalent Inhibitors of Fatty Acid Amide Hydrolase (Faah). Proc.Natl.Acad.Sci.Usa V. 108 7379 2011.
ISSN: ISSN 0027-8424
PubMed: 21502526
DOI: 10.1073/PNAS.1016167108