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Zinc in PDB 4rsy: Crystal Structures of the Human Leukotriene A4 Hydrolase Complex with A Potential Inhibitor H7

Enzymatic activity of Crystal Structures of the Human Leukotriene A4 Hydrolase Complex with A Potential Inhibitor H7

All present enzymatic activity of Crystal Structures of the Human Leukotriene A4 Hydrolase Complex with A Potential Inhibitor H7:
3.3.2.6;

Protein crystallography data

The structure of Crystal Structures of the Human Leukotriene A4 Hydrolase Complex with A Potential Inhibitor H7, PDB code: 4rsy was solved by P.Ouyang, W.Lu, K.Cui, J.Huang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.65 / 1.93
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 76.961, 86.803, 98.207, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 24.8

Other elements in 4rsy:

The structure of Crystal Structures of the Human Leukotriene A4 Hydrolase Complex with A Potential Inhibitor H7 also contains other interesting chemical elements:

Ytterbium (Yb) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structures of the Human Leukotriene A4 Hydrolase Complex with A Potential Inhibitor H7 (pdb code 4rsy). 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 Crystal Structures of the Human Leukotriene A4 Hydrolase Complex with A Potential Inhibitor H7, PDB code: 4rsy:

Zinc binding site 1 out of 1 in 4rsy

Go back to Zinc Binding Sites List in 4rsy
Zinc binding site 1 out of 1 in the Crystal Structures of the Human Leukotriene A4 Hydrolase Complex with A Potential Inhibitor H7


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structures of the Human Leukotriene A4 Hydrolase Complex with A Potential Inhibitor H7 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn702

b:15.0
occ:1.00
 O2 A:B3N701 1.9 15.7 1.0
O4 A:B3N701 2.0 14.8 1.0
OE1 A:GLU318 2.1 13.5 1.0
NE2 A:HIS299 2.1 13.8 1.0
CE1 A:HIS295 2.2 14.7 1.0
C1 A:B3N701 2.7 16.4 1.0
N3 A:B3N701 2.8 16.9 1.0
CD A:GLU318 2.8 15.3 1.0
OE2 A:GLU318 2.9 19.6 1.0
NE2 A:HIS295 3.1 15.8 1.0
CE1 A:HIS299 3.1 11.8 1.0
O A:HOH887 3.2 23.0 1.0
CD2 A:HIS299 3.2 11.5 1.0
ND1 A:HIS295 3.2 15.4 1.0
CE2 A:TYR383 3.9 13.7 1.0
OE1 A:GLU271 4.1 16.5 1.0
OH A:TYR383 4.1 12.8 1.0
C5 A:B3N701 4.2 15.3 1.0
ND1 A:HIS299 4.2 11.7 1.0
CD2 A:HIS295 4.3 13.6 1.0
CG A:GLU318 4.3 15.1 1.0
CG A:HIS299 4.3 11.6 1.0
CG A:HIS295 4.3 14.3 1.0
CZ A:TYR383 4.5 12.1 1.0
OE1 A:GLU296 4.5 14.9 1.0
CD A:GLU271 4.7 16.0 1.0
O A:HOH928 4.7 31.9 1.0
OE2 A:GLU296 4.7 14.0 1.0
CG2 A:THR321 4.7 10.6 1.0
O A:HOH846 4.8 18.2 1.0
OE2 A:GLU271 4.8 16.4 1.0
C6 A:B3N701 4.9 16.8 1.0
CB A:GLU318 4.9 14.8 1.0
CD2 A:TYR383 5.0 13.2 1.0

Reference:

P.Ouyang, W.Lu, K.Cui, J.Huang. Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor H1 To Be Published.
Page generated: Wed Dec 16 05:46:16 2020

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