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Ytterbium 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:

Zinc (Zn) 1 atom

Ytterbium Binding Sites:

The binding sites of Ytterbium 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 Ytterbium atom.
In total 3 binding sites of Ytterbium where determined in the Crystal Structure of Leukotriene A4 Hydrolase in Complex with N5-[4- (Phenylmethoxy)Phenyl]-L-Glutamine, PDB code: 3chq:
Jump to Ytterbium binding site number: 1; 2; 3;

Ytterbium binding site 1 out of 3 in 3chq

Go back to Ytterbium Binding Sites List in 3chq
Ytterbium binding site 1 out of 3 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 Ytterbium with other atoms in the Yb 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:Yb801

b:20.1
occ:1.00
 O A:HOH1582 2.3 16.3 1.0
OD1 A:ASP481 2.4 22.1 1.0
O A:HOH1583 2.4 10.5 1.0
O A:HOH1585 2.5 17.8 1.0
OD2 A:ASP481 2.7 30.2 1.0
CG A:ASP481 2.9 30.8 1.0
OD2 A:ASP482 4.2 19.1 1.0
OD1 A:ASP482 4.2 19.8 1.0
CB A:ASP481 4.4 28.8 1.0
O A:HOH1586 4.5 27.5 1.0
CG A:ASP482 4.6 19.9 1.0
O A:HOH1584 4.6 20.7 1.0
O A:HOH1489 4.7 25.1 1.0

Ytterbium binding site 2 out of 3 in 3chq

Go back to Ytterbium Binding Sites List in 3chq
Ytterbium binding site 2 out of 3 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 Ytterbium with other atoms in the Yb binding site number 2 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:Yb802

b:40.8
occ:0.50
 YB A:YB803 3.5 26.6 0.5
OE2 A:GLU107 4.8 52.4 1.0

Ytterbium binding site 3 out of 3 in 3chq

Go back to Ytterbium Binding Sites List in 3chq
Ytterbium binding site 3 out of 3 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 Ytterbium with other atoms in the Yb binding site number 3 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:Yb803

b:26.6
occ:0.50
 OE1 A:GLU107 2.4 54.5 1.0
OE2 A:GLU107 2.7 52.4 1.0
CD A:GLU107 2.9 51.5 1.0
YB A:YB802 3.5 40.8 0.5
CG A:GLU107 4.4 47.9 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 02:41:34 2020

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