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Zinc in PDB 3b7t: [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate

Enzymatic activity of [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate

All present enzymatic activity of [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate:
3.3.2.6;

Protein crystallography data

The structure of [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate, PDB code: 3b7t was solved by F.Tholander, J.Haeggstrom, M.Thunnissen, A.Muroya, B.-P.Roques, M.-C.Fournie-Zaluski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 78.490, 87.785, 99.916, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 27.3

Other elements in 3b7t:

The structure of [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate also contains other interesting chemical elements:

Ytterbium (Yb) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate (pdb code 3b7t). 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 [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate, PDB code: 3b7t:

Zinc binding site 1 out of 1 in 3b7t

Go back to Zinc Binding Sites List in 3b7t
Zinc binding site 1 out of 1 in the [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of [E296Q]LTA4H in Complex with Arg-Ala-Arg Substrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:41.0
occ:1.00
NE2 A:HIS295 2.1 34.4 1.0
OE1 A:GLU318 2.1 40.7 1.0
NE2 A:HIS299 2.2 39.5 1.0
N B:ARG702 2.3 58.8 1.0
O B:ARG702 2.5 42.8 1.0
OE2 A:GLU318 2.6 49.8 1.0
CD A:GLU318 2.7 44.0 1.0
C B:ARG702 2.9 44.1 1.0
CA B:ARG702 3.0 47.5 1.0
CE1 A:HIS295 3.0 42.6 1.0
CE1 A:HIS299 3.1 35.3 1.0
CD2 A:HIS295 3.1 34.6 1.0
CD2 A:HIS299 3.2 34.3 1.0
N B:ALA703 4.0 44.5 1.0
OE2 A:GLU271 4.1 80.6 1.0
ND1 A:HIS295 4.2 35.8 1.0
CG A:GLU318 4.2 45.8 1.0
CE2 A:TYR383 4.2 39.7 1.0
CG A:HIS295 4.2 44.8 1.0
ND1 A:HIS299 4.2 46.8 1.0
CG A:HIS299 4.3 33.6 1.0
CB B:ARG702 4.4 58.6 1.0
OH A:TYR383 4.5 46.1 1.0
CG2 A:THR321 4.5 39.0 1.0
CD A:GLU271 4.7 66.7 1.0
CA B:ALA703 4.7 50.2 1.0
OE1 A:GLU271 4.7 60.0 1.0
CZ A:TYR383 4.9 44.5 1.0
CB A:GLU318 4.9 42.0 1.0
CG B:ARG702 4.9 51.8 1.0
CA A:GLU318 5.0 40.4 1.0

Reference:

F.Tholander, A.Muroya, B.P.Roques, M.C.Fournie-Zaluski, M.M.Thunnissen, J.Z.Haeggstrom. Structure-Based Dissection of the Active Site Chemistry of Leukotriene A4 Hydrolase: Implications For M1 Aminopeptidases and Inhibitor Design. Chem.Biol. V. 15 920 2008.
ISSN: ISSN 1074-5521
PubMed: 18804029
DOI: 10.1016/J.CHEMBIOL.2008.07.018
Page generated: Wed Dec 16 04:08:39 2020

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