Ytterbium in PDB 1hs6: Structure of Leukotriene A4 Hydrolase Complexed with Bestatin.

All present enzymatic activity of Structure of Leukotriene A4 Hydrolase Complexed with Bestatin.:
3.3.2.6;

The structure of Structure of Leukotriene A4 Hydrolase Complexed with Bestatin., PDB code: 1hs6 was solved by M.M.G.M.Thunnissen, P.N.Nordlund, J.Z.Haeggstrom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.95
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	67.600, 133.500, 83.400, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of Structure of Leukotriene A4 Hydrolase Complexed with Bestatin. also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Ytterbium atom in the Structure of Leukotriene A4 Hydrolase Complexed with Bestatin. (pdb code 1hs6). This binding sites where shown within 5.0 Angstroms radius around Ytterbium atom.
In total 3 binding sites of Ytterbium where determined in the Structure of Leukotriene A4 Hydrolase Complexed with Bestatin., PDB code: 1hs6:
Jump to Ytterbium binding site number: 1; 2; 3;

Ytterbium binding site 1 out of 3 in the Structure of Leukotriene A4 Hydrolase Complexed with Bestatin.


Mono view


Stereo pair view

A full contact list of Ytterbium with other atoms in the Yb binding site number 1 of Structure of Leukotriene A4 Hydrolase Complexed with Bestatin. within 5.0Å range: probe atom residue distance (Å) B Occ A:Yb801 b:18.1 occ:1.00 OD1 A:ASP481 2.2 22.3 1.0 O A:HOH1260 2.2 13.9 1.0 OD2 A:ASP481 2.4 19.4 1.0 CG A:ASP481 2.6 26.7 1.0 OD1 A:ASP482 4.1 16.9 1.0 CB A:ASP481 4.1 22.4 1.0 OD2 A:ASP482 4.3 17.6 1.0 CG A:ASP482 4.6 14.6 1.0 CB A:LYS479 4.6 17.7 1.0 CD A:LYS479 4.8 28.8 1.0

Ytterbium binding site 2 out of 3 in the Structure of Leukotriene A4 Hydrolase Complexed with Bestatin.


Mono view


Stereo pair view

A full contact list of Ytterbium with other atoms in the Yb binding site number 2 of Structure of Leukotriene A4 Hydrolase Complexed with Bestatin. within 5.0Å range: probe atom residue distance (Å) B Occ A:Yb802 b:46.5 occ:0.50 YB A:YB803 3.4 30.2 0.5 OE1 A:GLU107 3.8 0.0 1.0 O A:HOH1409 3.9 54.6 1.0 OE2 A:GLU107 4.1 86.4 1.0 CD A:GLU107 4.3 0.0 1.0

Ytterbium binding site 3 out of 3 in the Structure of Leukotriene A4 Hydrolase Complexed with Bestatin.


Mono view


Stereo pair view

A full contact list of Ytterbium with other atoms in the Yb binding site number 3 of Structure of Leukotriene A4 Hydrolase Complexed with Bestatin. within 5.0Å range: probe atom residue distance (Å) B Occ A:Yb803 b:30.2 occ:0.50 OE2 A:GLU107 2.2 86.4 1.0 CD A:GLU107 2.7 0.0 1.0 OE1 A:GLU107 2.7 0.0 1.0 O A:HOH1409 2.9 54.6 1.0 YB A:YB802 3.4 46.5 0.5 CG A:GLU107 4.0 64.9 1.0 O A:HOH1303 4.7 41.0 1.0

M.M.Thunnissen, P.Nordlund, J.Z.Haeggstrom. Crystal Structure of Human Leukotriene A(4) Hydrolase, A Bifunctional Enzyme in Inflammation. Nat.Struct.Biol. V. 8 131 2001.
ISSN: ISSN 1072-8368
PubMed: 11175901
DOI: 10.1038/84117