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Zinc in PDB 2vj8: Complex of Human Leukotriene A4 Hydrolase with A Hydroxamic Acid Inhibitor

Enzymatic activity of Complex of Human Leukotriene A4 Hydrolase with A Hydroxamic Acid Inhibitor

All present enzymatic activity of Complex of Human Leukotriene A4 Hydrolase with A Hydroxamic Acid Inhibitor:
3.3.2.6;

Protein crystallography data

The structure of Complex of Human Leukotriene A4 Hydrolase with A Hydroxamic Acid Inhibitor, PDB code: 2vj8 was solved by M.M.G.M.Thunnissen, B.Andersson, C.-H.Wong, B.Samuelsson, J.Z.Haeggstrom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.80
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 67.770, 132.470, 83.700, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / 23.5

Other elements in 2vj8:

The structure of Complex of Human Leukotriene A4 Hydrolase with A Hydroxamic Acid Inhibitor also contains other interesting chemical elements:

Ytterbium (Yb) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Complex of Human Leukotriene A4 Hydrolase with A Hydroxamic Acid Inhibitor (pdb code 2vj8). 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 Complex of Human Leukotriene A4 Hydrolase with A Hydroxamic Acid Inhibitor, PDB code: 2vj8:

Zinc binding site 1 out of 1 in 2vj8

Go back to Zinc Binding Sites List in 2vj8
Zinc binding site 1 out of 1 in the Complex of Human Leukotriene A4 Hydrolase with A Hydroxamic Acid Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Complex of Human Leukotriene A4 Hydrolase with A Hydroxamic Acid Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1611

b:17.6
occ:1.00
OE1 A:GLU318 2.0 13.2 1.0
NE2 A:HIS299 2.0 13.7 1.0
O2 A:HA21616 2.0 28.8 1.0
NE2 A:HIS295 2.0 13.8 1.0
CD A:GLU318 2.7 16.3 1.0
OE2 A:GLU318 2.7 22.2 1.0
N3 A:HA21616 2.9 37.0 1.0
CE1 A:HIS299 2.9 14.2 1.0
CD2 A:HIS299 3.0 13.7 1.0
CE1 A:HIS295 3.0 16.0 1.0
CD2 A:HIS295 3.0 16.0 1.0
C16 A:HA21616 3.5 25.8 1.0
CE2 A:TYR383 3.7 18.4 1.0
C17 A:HA21616 3.8 30.5 1.0
N2 A:HA21616 3.9 29.4 1.0
OH A:TYR383 4.0 16.5 1.0
C18 A:HA21616 4.0 26.4 1.0
ND1 A:HIS299 4.0 15.6 1.0
CG A:HIS299 4.1 16.8 1.0
ND1 A:HIS295 4.1 14.4 1.0
CG A:GLU318 4.2 15.5 1.0
CG A:HIS295 4.2 15.4 1.0
CZ A:TYR383 4.3 20.8 1.0
C15 A:HA21616 4.3 28.6 1.0
CG2 A:THR321 4.4 12.7 1.0
O A:HOH2270 4.5 16.4 1.0
OE1 A:GLU271 4.6 18.5 1.0
CD2 A:TYR383 4.7 11.2 1.0
CB A:THR321 4.7 11.1 1.0
OE1 A:GLU296 4.7 21.3 1.0
O3 A:HA21616 4.8 24.9 1.0
CB A:GLU318 4.8 13.7 1.0
CA A:GLU318 4.9 11.1 1.0
OE2 A:GLU271 4.9 19.5 1.0
C14 A:HA21616 5.0 20.8 1.0
CD A:GLU271 5.0 24.4 1.0

Reference:

M.M.G.M.Thunnissen, B.Andersson, C.-H.Wong, B.Samuelsson, J.Z.Haeggstrom. Crystal Structures of Leukotriene A4 Hydrolase in Complex with Captopril and Two Competitive Tight-Binding Inhibitors Faseb J. V. 16 1648 2002.
ISSN: ISSN 0892-6638
PubMed: 12207002
DOI: 10.1096/FJ.01-1017FJE
Page generated: Wed Dec 16 03:55:14 2020

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