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Ytterbium in PDB 1gw6: Structure of Leukotriene A4 Hydrolase D375N Mutant

Enzymatic activity of Structure of Leukotriene A4 Hydrolase D375N Mutant

All present enzymatic activity of Structure of Leukotriene A4 Hydrolase D375N Mutant:
3.3.2.6;

Protein crystallography data

The structure of Structure of Leukotriene A4 Hydrolase D375N Mutant, PDB code: 1gw6 was solved by P.C.Rudberg, F.Tholander, M.M.G.M.Thunnissen, B.Samuelsson, J.Z.Haeggstrom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.95 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 78.430, 87.060, 99.070, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 22

Other elements in 1gw6:

The structure of Structure of Leukotriene A4 Hydrolase D375N Mutant also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Ytterbium Binding Sites:

The binding sites of Ytterbium atom in the Structure of Leukotriene A4 Hydrolase D375N Mutant (pdb code 1gw6). This binding sites where shown within 5.0 Angstroms radius around Ytterbium atom.
In total only one binding site of Ytterbium was determined in the Structure of Leukotriene A4 Hydrolase D375N Mutant, PDB code: 1gw6:

Ytterbium binding site 1 out of 1 in 1gw6

Go back to Ytterbium Binding Sites List in 1gw6
Ytterbium binding site 1 out of 1 in the Structure of Leukotriene A4 Hydrolase D375N Mutant


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 D375N Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Yb1614

b:30.6
occ:1.00
OD2 A:ASP481 2.7 14.4 1.0
OD1 A:ASP481 2.7 16.6 1.0
O A:HOH2356 2.8 21.6 1.0
O A:HOH2355 2.8 24.5 1.0
CG A:ASP481 3.0 19.0 1.0
OD2 A:ASP482 4.4 16.0 1.0
OD1 A:ASP482 4.5 22.5 1.0
CB A:ASP481 4.5 16.3 1.0
CG A:ASP482 4.7 17.1 1.0
CB A:LYS479 4.7 17.7 1.0
CG A:LYS479 4.9 18.1 1.0

Reference:

P.C.Rudberg, F.Tholander, M.M.G.M.Thunnissen, B.Samuelsson, J.Z.Haeggstrom. Leukotriene A4 Hydrolase: Selective Abrogation of Leukotriene B4 Formation By Mutation of Aspartic Acid 375 Proc.Natl.Acad.Sci.Usa V. 99 4215 2002.
ISSN: ISSN 0027-8424
PubMed: 11917124
DOI: 10.1073/PNAS.072090099
Page generated: Sat Oct 12 20:53:49 2024

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