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Zinc in PDB 3b7s: [E296Q]LTA4H in Complex with Rsr Substrate

Enzymatic activity of [E296Q]LTA4H in Complex with Rsr Substrate

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

Protein crystallography data

The structure of [E296Q]LTA4H in Complex with Rsr Substrate, PDB code: 3b7s 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) 10.00 / 1.47
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 78.508, 87.351, 99.769, 90.00, 90.00, 90.00
R / Rfree (%) 12.8 / 16.9

Other elements in 3b7s:

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

Ytterbium (Yb) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the [E296Q]LTA4H in Complex with Rsr Substrate (pdb code 3b7s). 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 Rsr Substrate, PDB code: 3b7s:

Zinc binding site 1 out of 1 in 3b7s

Go back to Zinc Binding Sites List in 3b7s
Zinc binding site 1 out of 1 in the [E296Q]LTA4H in Complex with Rsr 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 Rsr Substrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:9.0
occ:1.00
OE1 A:GLU318 2.0 10.0 1.0
NE2 A:HIS295 2.0 8.7 1.0
N B:ARG800 2.0 11.0 1.0
NE2 A:HIS299 2.1 8.2 1.0
O B:ARG800 2.6 9.4 1.0
CD A:GLU318 2.7 9.7 1.0
OE2 A:GLU318 2.8 12.1 1.0
CD2 A:HIS295 3.0 8.2 1.0
C B:ARG800 3.1 9.4 1.0
CD2 A:HIS299 3.1 6.5 1.0
CA B:ARG800 3.1 8.7 1.0
CE1 A:HIS295 3.1 9.5 1.0
CE1 A:HIS299 3.1 9.8 1.0
CE2 A:TYR383 4.1 10.7 1.0
OE2 A:GLU271 4.2 9.9 1.0
CG A:GLU318 4.2 9.6 1.0
N B:SER801 4.2 9.2 1.0
ND1 A:HIS295 4.2 9.3 1.0
CG A:HIS299 4.2 8.9 1.0
CG A:HIS295 4.2 9.9 1.0
ND1 A:HIS299 4.2 8.8 1.0
O A:HOH1091 4.3 10.8 1.0
CB B:ARG800 4.3 10.7 1.0
OH A:TYR383 4.4 10.9 1.0
NE2 A:GLN296 4.5 7.2 1.0
CG2 A:THR321 4.5 9.0 1.0
OE1 A:GLU271 4.6 11.2 1.0
CD A:GLU271 4.7 10.4 1.0
CZ A:TYR383 4.7 9.6 1.0
CB A:GLU318 4.8 10.5 1.0
CA A:GLU318 4.8 9.8 1.0
CG B:ARG800 4.8 10.2 1.0
CB A:THR321 4.9 8.2 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 04:08:40 2020

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