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Zinc in PDB 3cho: Crystal Structure of Leukotriene A4 Hydrolase in Complex with 2-Amino- N-[4-(Phenylmethoxy)Phenyl]-Acetamide

Enzymatic activity of Crystal Structure of Leukotriene A4 Hydrolase in Complex with 2-Amino- N-[4-(Phenylmethoxy)Phenyl]-Acetamide

All present enzymatic activity of Crystal Structure of Leukotriene A4 Hydrolase in Complex with 2-Amino- N-[4-(Phenylmethoxy)Phenyl]-Acetamide:
3.3.2.6;

Protein crystallography data

The structure of Crystal Structure of Leukotriene A4 Hydrolase in Complex with 2-Amino- N-[4-(Phenylmethoxy)Phenyl]-Acetamide, PDB code: 3cho 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) 14.74 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 78.312, 87.124, 99.364, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Other elements in 3cho:

The structure of Crystal Structure of Leukotriene A4 Hydrolase in Complex with 2-Amino- N-[4-(Phenylmethoxy)Phenyl]-Acetamide also contains other interesting chemical elements:

Ytterbium (Yb) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Leukotriene A4 Hydrolase in Complex with 2-Amino- N-[4-(Phenylmethoxy)Phenyl]-Acetamide (pdb code 3cho). 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 2-Amino- N-[4-(Phenylmethoxy)Phenyl]-Acetamide, PDB code: 3cho:

Zinc binding site 1 out of 1 in 3cho

Go back to Zinc Binding Sites List in 3cho
Zinc binding site 1 out of 1 in the Crystal Structure of Leukotriene A4 Hydrolase in Complex with 2-Amino- N-[4-(Phenylmethoxy)Phenyl]-Acetamide


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 2-Amino- N-[4-(Phenylmethoxy)Phenyl]-Acetamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:17.5
occ:1.00
 NE2 A:HIS299 2.1 13.4 1.0
NE2 A:HIS295 2.1 12.6 1.0
OE1 A:GLU318 2.1 16.6 1.0
O A:HOH1006 2.2 17.0 1.0
OE2 A:GLU318 2.6 16.0 1.0
CD A:GLU318 2.7 17.1 1.0
CD2 A:HIS295 3.1 14.0 1.0
CE1 A:HIS299 3.1 10.8 1.0
CD2 A:HIS299 3.1 13.9 1.0
CE1 A:HIS295 3.1 12.6 1.0
O A:HOH1115 3.1 39.3 1.0
CE2 A:TYR383 3.8 17.3 1.0
O A:HOH1008 3.9 12.7 1.0
OH A:TYR383 4.0 18.3 1.0
CG A:GLU318 4.1 14.9 1.0
ND1 A:HIS299 4.2 12.5 1.0
CG A:HIS295 4.2 15.3 1.0
CG A:HIS299 4.2 11.2 1.0
ND1 A:HIS295 4.2 16.9 1.0
CZ A:TYR383 4.3 19.2 1.0
CG2 A:THR321 4.4 10.2 1.0
OE2 A:GLU271 4.5 15.6 1.0
O A:HOH1066 4.5 14.0 1.0
CD2 A:TYR383 4.7 13.6 1.0
CB A:THR321 4.8 12.2 1.0
CB A:GLU318 4.8 14.5 1.0
CA A:GLU318 4.9 14.5 1.0
OE1 A:GLU271 4.9 15.3 1.0
CD A:GLU271 4.9 14.3 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 04:10:38 2020

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