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Zinc in PDB 3chq: Crystal Structure of Leukotriene A4 Hydrolase in Complex with N5-[4- (Phenylmethoxy)Phenyl]-L-Glutamine

Enzymatic activity of Crystal Structure of Leukotriene A4 Hydrolase in Complex with N5-[4- (Phenylmethoxy)Phenyl]-L-Glutamine

All present enzymatic activity of Crystal Structure of Leukotriene A4 Hydrolase in Complex with N5-[4- (Phenylmethoxy)Phenyl]-L-Glutamine:
3.3.2.6;

Protein crystallography data

The structure of Crystal Structure of Leukotriene A4 Hydrolase in Complex with N5-[4- (Phenylmethoxy)Phenyl]-L-Glutamine, PDB code: 3chq was solved by M.M.G.M.Thunnissen, M.Adler, M.Whitlow, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.83 / 2.09
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 68.234, 133.262, 84.591, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Other elements in 3chq:

The structure of Crystal Structure of Leukotriene A4 Hydrolase in Complex with N5-[4- (Phenylmethoxy)Phenyl]-L-Glutamine also contains other interesting chemical elements:

Ytterbium (Yb) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Leukotriene A4 Hydrolase in Complex with N5-[4- (Phenylmethoxy)Phenyl]-L-Glutamine (pdb code 3chq). 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 Crystal Structure of Leukotriene A4 Hydrolase in Complex with N5-[4- (Phenylmethoxy)Phenyl]-L-Glutamine, PDB code: 3chq:

Zinc binding site 1 out of 1 in 3chq

Go back to Zinc Binding Sites List in 3chq
Zinc binding site 1 out of 1 in the Crystal Structure of Leukotriene A4 Hydrolase in Complex with N5-[4- (Phenylmethoxy)Phenyl]-L-Glutamine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Leukotriene A4 Hydrolase in Complex with N5-[4- (Phenylmethoxy)Phenyl]-L-Glutamine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:17.1
occ:1.00
OE1 A:GLU318 2.1 13.0 1.0
NE2 A:HIS299 2.1 16.1 1.0
O1 A:4BQ901 2.1 22.9 1.0
NE2 A:HIS295 2.2 16.3 1.0
CD A:GLU318 2.8 15.7 1.0
OE2 A:GLU318 2.9 16.1 1.0
CE1 A:HIS299 3.0 15.4 1.0
C2 A:4BQ901 3.0 24.0 1.0
CE1 A:HIS295 3.1 12.7 1.0
CD2 A:HIS295 3.1 10.6 1.0
CD2 A:HIS299 3.1 18.5 1.0
O3 A:4BQ901 3.5 27.9 1.0
CE2 A:TYR383 3.6 12.2 1.0
OH A:TYR383 4.0 13.0 1.0
N5 A:4BQ901 4.1 25.1 1.0
ND1 A:HIS299 4.2 20.7 1.0
CZ A:TYR383 4.2 12.1 1.0
C4 A:4BQ901 4.2 24.9 1.0
ND1 A:HIS295 4.2 16.1 1.0
CG A:GLU318 4.2 12.6 1.0
CG A:HIS299 4.3 18.8 1.0
CG A:HIS295 4.3 13.2 1.0
CD2 A:TYR383 4.5 12.9 1.0
CG2 A:THR321 4.5 13.0 1.0
O A:HOH1100 4.6 15.1 1.0
OE1 A:GLU271 4.6 18.4 1.0
CB A:THR321 4.7 16.5 1.0
CA A:GLU318 4.8 15.5 1.0
CB A:GLU318 4.8 15.4 1.0
OE2 A:GLU271 4.9 17.8 1.0
CD A:GLU271 5.0 20.5 1.0

Reference:

T.A.Kirkland, M.Adler, J.G.Bauman, M.Chen, J.Z.Haeggstrom, B.King, M.J.Kochanny, A.M.Liang, L.Mendoza, G.B.Phillips, M.Thunnissen, L.Trinh, M.Whitlow, B.Ye, H.Ye, J.Parkinson, W.J.Guilford. Synthesis of Glutamic Acid Analogs As Potent Inhibitors of Leukotriene A4 Hydrolase. Bioorg.Med.Chem. V. 16 4963 2008.
ISSN: ISSN 0968-0896
PubMed: 18394906
DOI: 10.1016/J.BMC.2008.03.042
Page generated: Wed Dec 16 04:10:41 2020

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