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Zinc in PDB 4l2l: Human Leukotriene A4 Hydrolase Complexed with Ligand 4-(4- Benzylphenyl)Thiazol-2-Amine

Enzymatic activity of Human Leukotriene A4 Hydrolase Complexed with Ligand 4-(4- Benzylphenyl)Thiazol-2-Amine

All present enzymatic activity of Human Leukotriene A4 Hydrolase Complexed with Ligand 4-(4- Benzylphenyl)Thiazol-2-Amine:
3.3.2.6;

Protein crystallography data

The structure of Human Leukotriene A4 Hydrolase Complexed with Ligand 4-(4- Benzylphenyl)Thiazol-2-Amine, PDB code: 4l2l was solved by A.Stsiapanava, A.Rinaldo-Matthis, J.Z.Haeggstrom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.18 / 1.65
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 66.171, 76.701, 67.215, 90.00, 98.43, 90.00
R / Rfree (%) 14.2 / 17.5

Other elements in 4l2l:

The structure of Human Leukotriene A4 Hydrolase Complexed with Ligand 4-(4- Benzylphenyl)Thiazol-2-Amine also contains other interesting chemical elements:

Ytterbium (Yb) 6 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Leukotriene A4 Hydrolase Complexed with Ligand 4-(4- Benzylphenyl)Thiazol-2-Amine (pdb code 4l2l). 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 Human Leukotriene A4 Hydrolase Complexed with Ligand 4-(4- Benzylphenyl)Thiazol-2-Amine, PDB code: 4l2l:

Zinc binding site 1 out of 1 in 4l2l

Go back to Zinc Binding Sites List in 4l2l
Zinc binding site 1 out of 1 in the Human Leukotriene A4 Hydrolase Complexed with Ligand 4-(4- Benzylphenyl)Thiazol-2-Amine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Leukotriene A4 Hydrolase Complexed with Ligand 4-(4- Benzylphenyl)Thiazol-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:6.7
occ:1.00
 O A:ACT707 1.9 12.7 1.0
OE2 A:GLU318 2.0 7.7 1.0
NE2 A:HIS295 2.0 6.1 1.0
NE2 A:HIS299 2.0 4.6 1.0
OXT A:ACT707 2.6 12.7 1.0
C A:ACT707 2.7 17.3 1.0
CD A:GLU318 2.7 7.3 1.0
OE1 A:GLU318 2.8 9.9 1.0
CE1 A:HIS299 2.9 5.0 1.0
CE1 A:HIS295 3.0 5.5 1.0
CD2 A:HIS295 3.1 6.2 1.0
CD2 A:HIS299 3.1 5.0 1.0
O A:HOH916 3.6 12.6 1.0
CE2 A:TYR383 3.7 8.0 1.0
OH A:TYR383 4.0 9.7 1.0
ND1 A:HIS299 4.1 4.7 1.0
ND1 A:HIS295 4.1 6.0 1.0
CH3 A:ACT707 4.1 21.4 1.0
CG A:HIS295 4.2 5.5 1.0
CG A:HIS299 4.2 4.4 1.0
CG A:GLU318 4.2 6.8 1.0
CZ A:TYR383 4.2 8.3 1.0
OE2 A:GLU271 4.3 7.2 1.0
CG2 A:THR321 4.4 6.5 1.0
CD2 A:TYR383 4.6 7.3 1.0
O A:HOH965 4.8 11.2 1.0
CB A:THR321 4.8 6.2 1.0
CB A:GLU318 4.8 6.2 1.0
OE1 A:GLU271 4.8 8.6 1.0
CD A:GLU271 4.8 6.8 1.0
OE2 A:GLU296 4.9 10.3 1.0
CA A:GLU318 4.9 6.1 1.0

Reference:

A.Stsiapanava, U.Olsson, M.Wan, T.Kleinschmidt, D.Rutishauser, R.A.Zubarev, B.Samuelsson, A.Rinaldo-Matthis, J.Z.Haeggstrom. Binding of Pro-Gly-Pro at the Active Site of Leukotriene A4 Hydrolase/Aminopeptidase and Development of An Epoxide Hydrolase Selective Inhibitor. Proc.Natl.Acad.Sci.Usa V. 111 4227 2014.
ISSN: ISSN 0027-8424
PubMed: 24591641
DOI: 10.1073/PNAS.1402136111
Page generated: Sun Oct 27 01:31:20 2024

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