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Zinc in PDB 4gaa: Structure of Leukotriene A4 Hydrolase From Xenopus Laevis Complexed with Inhibitor Bestatin

Enzymatic activity of Structure of Leukotriene A4 Hydrolase From Xenopus Laevis Complexed with Inhibitor Bestatin

All present enzymatic activity of Structure of Leukotriene A4 Hydrolase From Xenopus Laevis Complexed with Inhibitor Bestatin:
3.3.2.6;

Protein crystallography data

The structure of Structure of Leukotriene A4 Hydrolase From Xenopus Laevis Complexed with Inhibitor Bestatin, PDB code: 4gaa was solved by A.Stsiapanava, R.B.Kumar, J.Z.Haeggstrom, A.Rinaldo-Matthis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.30 / 2.26
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 222.120, 52.170, 109.900, 90.00, 111.58, 90.00
R / Rfree (%) 22.2 / 25

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Leukotriene A4 Hydrolase From Xenopus Laevis Complexed with Inhibitor Bestatin (pdb code 4gaa). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Leukotriene A4 Hydrolase From Xenopus Laevis Complexed with Inhibitor Bestatin, PDB code: 4gaa:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4gaa

Go back to Zinc Binding Sites List in 4gaa
Zinc binding site 1 out of 2 in the Structure of Leukotriene A4 Hydrolase From Xenopus Laevis Complexed with Inhibitor Bestatin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Leukotriene A4 Hydrolase From Xenopus Laevis Complexed with Inhibitor Bestatin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:44.4
occ:1.00
OE2 A:GLU315 1.9 44.0 1.0
NE2 A:HIS292 2.0 40.4 1.0
NE2 A:HIS296 2.2 42.9 1.0
OE1 A:GLU315 2.3 41.7 1.0
CD A:GLU315 2.4 63.6 1.0
O3 A:BES702 2.5 51.8 1.0
O2 A:BES702 2.6 43.6 1.0
CE1 A:HIS292 2.9 42.3 1.0
C3 A:BES702 3.1 48.5 1.0
CD2 A:HIS296 3.1 41.3 1.0
CD2 A:HIS292 3.1 40.3 1.0
C2 A:BES702 3.1 42.8 1.0
CE1 A:HIS296 3.2 43.1 1.0
C1 A:BES702 3.7 38.9 1.0
CG A:GLU315 3.9 48.1 1.0
ND1 A:HIS292 4.1 43.8 1.0
CG A:HIS292 4.2 41.6 1.0
N1 A:BES702 4.2 52.4 1.0
CG A:HIS296 4.3 40.2 1.0
OE1 A:GLU293 4.3 68.8 1.0
OH A:TYR380 4.3 66.6 1.0
ND1 A:HIS296 4.3 42.9 1.0
N2 A:BES702 4.4 33.0 1.0
CE2 A:TYR380 4.4 57.3 1.0
OE1 A:GLU268 4.4 49.9 1.0
CG2 A:THR318 4.5 39.3 1.0
OE2 A:GLU293 4.6 61.6 1.0
CZ A:TYR380 4.7 65.2 1.0
CD A:GLU293 4.8 69.6 1.0
OE2 A:GLU268 4.9 45.8 1.0
CB A:GLU315 4.9 46.1 1.0
CD A:GLU268 4.9 58.1 1.0
O A:HOH812 4.9 42.6 1.0

Zinc binding site 2 out of 2 in 4gaa

Go back to Zinc Binding Sites List in 4gaa
Zinc binding site 2 out of 2 in the Structure of Leukotriene A4 Hydrolase From Xenopus Laevis Complexed with Inhibitor Bestatin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Leukotriene A4 Hydrolase From Xenopus Laevis Complexed with Inhibitor Bestatin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn701

b:55.9
occ:1.00
OE2 B:GLU315 2.0 60.6 1.0
O2 B:BES702 2.1 64.1 1.0
OE1 B:GLU315 2.1 42.0 1.0
NE2 B:HIS292 2.2 58.5 1.0
CD B:GLU315 2.4 64.1 1.0
NE2 B:HIS296 2.4 57.2 1.0
O3 B:BES702 2.6 72.2 1.0
CD2 B:HIS296 2.9 59.1 1.0
CD2 B:HIS292 3.0 61.4 1.0
C2 B:BES702 3.1 66.6 1.0
C3 B:BES702 3.2 70.7 1.0
CE1 B:HIS292 3.3 55.0 1.0
CE1 B:HIS296 3.7 55.5 1.0
C1 B:BES702 3.8 63.4 1.0
CG B:GLU315 3.9 54.5 1.0
OE1 B:GLU293 4.0 71.4 1.0
N2 B:BES702 4.1 64.4 1.0
CG B:HIS296 4.1 57.2 1.0
CG B:HIS292 4.2 57.9 1.0
CG2 B:THR318 4.2 42.7 1.0
OE1 B:GLU268 4.2 54.9 1.0
ND1 B:HIS292 4.4 56.0 1.0
CE1 B:TYR380 4.4 51.3 1.0
N1 B:BES702 4.4 72.0 1.0
ND1 B:HIS296 4.5 56.9 1.0
OE2 B:GLU293 4.6 88.3 1.0
OH B:TYR380 4.6 65.4 1.0
CB B:THR318 4.7 43.4 1.0
CD B:GLU293 4.7 89.8 1.0
CB B:GLU315 4.8 46.1 1.0
CZ B:TYR380 4.9 59.8 1.0
CA B:GLU315 4.9 42.9 1.0
CD B:GLU268 5.0 74.0 1.0

Reference:

A.Stsiapanava, F.Tholander, R.B.Kumar, A.A.Qureshi, D.Niegowski, M.Hasan, M.Thunnissen, J.Z.Haeggstrom, A.Rinaldo-Matthis. Product Formation Controlled By Substrate Dynamics in Leukotriene A4 Hydrolase. Biochim.Biophys.Acta V.1844 439 2014.
ISSN: ISSN 0006-3002
PubMed: 24333438
DOI: 10.1016/J.BBAPAP.2013.12.003
Page generated: Wed Dec 16 05:19:31 2020

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