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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 1hs6:

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

Ytterbium (Yb) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the Structure of Leukotriene A4 Hydrolase Complexed with Bestatin., PDB code: 1hs6:

Zinc binding site 1 out of 1 in 1hs6

Go back to Zinc Binding Sites List in 1hs6
Zinc binding site 1 out of 1 in the Structure of Leukotriene A4 Hydrolase Complexed with Bestatin.


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 Complexed with Bestatin. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:16.3
occ:1.00
OE1 A:GLU318 1.9 13.0 1.0
NE2 A:HIS295 2.0 13.9 1.0
NE2 A:HIS299 2.0 13.6 1.0
O2 A:BES901 2.1 18.6 1.0
O3 A:BES901 2.5 25.7 1.0
CD A:GLU318 2.7 14.8 1.0
OE2 A:GLU318 2.8 13.6 1.0
CD2 A:HIS299 2.9 14.1 1.0
C2 A:BES901 3.0 21.8 1.0
CD2 A:HIS295 3.0 14.2 1.0
C3 A:BES901 3.0 23.3 1.0
CE1 A:HIS295 3.0 12.2 1.0
CE1 A:HIS299 3.1 13.4 1.0
C1 A:BES901 3.5 24.1 1.0
N2 A:BES901 3.9 25.7 1.0
OE1 A:GLU296 4.0 19.0 1.0
CG A:HIS295 4.1 14.9 1.0
CE2 A:TYR383 4.1 10.2 1.0
CG A:HIS299 4.1 18.4 1.0
ND1 A:HIS295 4.1 13.2 1.0
ND1 A:HIS299 4.2 15.2 1.0
CG A:GLU318 4.2 8.2 1.0
N1 A:BES901 4.2 21.9 1.0
OH A:TYR383 4.2 12.6 1.0
OE1 A:GLU271 4.4 16.5 1.0
O A:HOH1230 4.5 17.1 1.0
CG2 A:THR321 4.5 12.3 1.0
OE2 A:GLU296 4.6 16.7 1.0
CZ A:TYR383 4.6 14.3 1.0
CD A:GLU296 4.6 15.9 1.0
CB A:THR321 4.7 19.1 1.0
OE2 A:GLU271 4.8 15.5 1.0
CD A:GLU271 4.8 16.6 1.0
CB A:GLU318 4.9 9.5 1.0
CA A:GLU318 4.9 12.0 1.0
C6 A:BES901 4.9 23.8 1.0
C4 A:BES901 5.0 24.2 1.0

Reference:

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
Page generated: Wed Dec 16 02:51:37 2020

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