Zinc in PDB 1h19: Structure of [E271Q]Leukotriene A4 Hydrolase

All present enzymatic activity of Structure of [E271Q]Leukotriene A4 Hydrolase:
3.3.2.6;

The structure of Structure of [E271Q]Leukotriene A4 Hydrolase, PDB code: 1h19 was solved by P.C.Rudberg, F.Tholander, M.M.G.M.Thunnissen, J.Z.Haeggstrom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.16 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	77.962, 86.873, 98.787, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 23.2

The structure of Structure of [E271Q]Leukotriene A4 Hydrolase also contains other interesting chemical elements:

Ytterbium

(Yb)

1 atom

The binding sites of Zinc atom in the Structure of [E271Q]Leukotriene A4 Hydrolase (pdb code 1h19). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of [E271Q]Leukotriene A4 Hydrolase, PDB code: 1h19:

Zinc binding site 1 out of 1 in the Structure of [E271Q]Leukotriene A4 Hydrolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of [E271Q]Leukotriene A4 Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:13.2 occ:1.00 OE1 A:GLU318 2.0 11.8 1.0 NE2 A:HIS299 2.0 12.0 1.0 O A:ACY901 2.1 12.5 1.0 NE2 A:HIS295 2.1 14.3 1.0 CD A:GLU318 2.7 9.9 1.0 C A:ACY901 2.8 12.2 1.0 OXT A:ACY901 2.8 13.2 1.0 OE2 A:GLU318 2.8 9.4 1.0 CE1 A:HIS299 2.9 10.2 1.0 CD2 A:HIS295 3.0 12.1 1.0 CE1 A:HIS295 3.1 12.4 1.0 CD2 A:HIS299 3.1 8.4 1.0 CE2 A:TYR383 3.7 13.4 1.0 O A:HOH2170 3.8 10.5 1.0 ND1 A:HIS299 4.1 10.6 1.0 OH A:TYR383 4.1 13.3 1.0 CG A:GLU318 4.2 11.0 1.0 CG A:HIS299 4.2 8.1 1.0 CG A:HIS295 4.2 14.4 1.0 ND1 A:HIS295 4.2 12.4 1.0 CH3 A:ACY901 4.2 11.2 1.0 CZ A:TYR383 4.3 13.4 1.0 NE2 A:GLN271 4.3 13.1 1.0 CG2 A:THR321 4.4 10.8 1.0 CD2 A:TYR383 4.6 11.7 1.0 CB A:THR321 4.7 9.3 1.0 CB A:GLU318 4.7 10.9 1.0 O A:HOH2305 4.8 11.3 1.0 CA A:GLU318 4.8 12.3 1.0 OE2 A:GLU296 4.9 17.7 1.0

P.C.Rudberg, F.Tholander, M.M.G.M.Thunnissen, J.Z.Haeggstrom. Leukotriene A4 Hydrolase/Aminopeptidase, Glutamate 271 Is A Catalyticresidue with Specific Roles in Two Distinct Enzyme Mechanisms J.Biol.Chem. V. 277 1398 2002.
ISSN: ISSN 0021-9258
PubMed: 11675384
DOI: 10.1074/JBC.M106577200