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Zinc 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:

Ytterbium (Yb) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Leukotriene A4 Hydrolase D375N Mutant (pdb code 1gw6). 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 Structure of Leukotriene A4 Hydrolase D375N Mutant, PDB code: 1gw6:

Zinc binding site 1 out of 1 in 1gw6

Go back to Zinc Binding Sites List in 1gw6
Zinc 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 Zinc with other atoms in the Zn binding site number 1 of Structure of Leukotriene A4 Hydrolase D375N Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1615

b:12.1
occ:1.00
NE2 A:HIS295 2.0 11.4 1.0
OE1 A:GLU318 2.0 12.3 1.0
O2 A:BES1611 2.1 15.1 1.0
NE2 A:HIS299 2.1 9.6 1.0
O3 A:BES1611 2.4 18.8 1.0
OE2 A:GLU318 2.6 9.5 1.0
CD A:GLU318 2.7 12.7 1.0
CE1 A:HIS295 2.9 10.6 1.0
C2 A:BES1611 2.9 14.7 1.0
C3 A:BES1611 3.0 17.1 1.0
CD2 A:HIS299 3.0 7.7 1.0
CD2 A:HIS295 3.1 7.6 1.0
CE1 A:HIS299 3.2 6.0 1.0
C1 A:BES1611 3.5 16.4 1.0
ND1 A:HIS295 4.0 9.4 1.0
N2 A:BES1611 4.0 17.9 1.0
CE2 A:TYR383 4.2 12.0 1.0
CG A:GLU318 4.2 10.1 1.0
CG A:HIS295 4.2 11.0 1.0
CG A:HIS299 4.2 10.3 1.0
N1 A:BES1611 4.2 20.7 1.0
ND1 A:HIS299 4.2 9.7 1.0
OH A:TYR383 4.4 16.1 1.0
OE1 A:GLU296 4.4 21.4 1.0
OE1 A:GLU271 4.4 14.9 1.0
CG2 A:THR321 4.4 7.3 1.0
OE2 A:GLU296 4.6 18.1 1.0
O A:HOH2138 4.6 14.3 1.0
CZ A:TYR383 4.7 13.4 1.0
CB A:GLU318 4.8 13.3 1.0
CB A:THR321 4.8 9.0 1.0
CA A:GLU318 4.8 13.6 1.0
OE2 A:GLU271 4.9 11.8 1.0
CD A:GLU271 4.9 14.6 1.0
CD A:GLU296 4.9 18.0 1.0
C6 A:BES1611 4.9 15.2 1.0
C14 A:BES1611 5.0 27.7 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: Wed Dec 16 02:50:26 2020

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