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Zinc in PDB 3b7u: Leukotriene A4 Hydrolase Complexed with Kelatorphan

Enzymatic activity of Leukotriene A4 Hydrolase Complexed with Kelatorphan

All present enzymatic activity of Leukotriene A4 Hydrolase Complexed with Kelatorphan:
3.3.2.6;

Protein crystallography data

The structure of Leukotriene A4 Hydrolase Complexed with Kelatorphan, PDB code: 3b7u 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) 14.67 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 77.829, 87.136, 99.191, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 21.7

Other elements in 3b7u:

The structure of Leukotriene A4 Hydrolase Complexed with Kelatorphan also contains other interesting chemical elements:

Ytterbium (Yb) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Leukotriene A4 Hydrolase Complexed with Kelatorphan (pdb code 3b7u). 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 Leukotriene A4 Hydrolase Complexed with Kelatorphan, PDB code: 3b7u:

Zinc binding site 1 out of 1 in 3b7u

Go back to Zinc Binding Sites List in 3b7u
Zinc binding site 1 out of 1 in the Leukotriene A4 Hydrolase Complexed with Kelatorphan


Mono view


Stereo pair view

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

b:6.7
occ:1.00
OE1 X:GLU318 2.0 5.8 1.0
NE2 X:HIS299 2.0 7.0 1.0
O21 X:KEL707 2.1 8.7 1.0
NE2 X:HIS295 2.1 7.9 1.0
O20 X:KEL707 2.3 19.7 1.0
CD X:GLU318 2.7 4.2 1.0
OE2 X:GLU318 2.7 7.8 1.0
C18 X:KEL707 2.8 12.2 1.0
N19 X:KEL707 3.0 13.8 1.0
CE1 X:HIS299 3.0 4.5 1.0
CD2 X:HIS299 3.0 4.5 1.0
CD2 X:HIS295 3.0 4.9 1.0
CE1 X:HIS295 3.1 5.1 1.0
O X:HOH822 3.8 14.1 1.0
CE2 X:TYR383 4.0 9.3 1.0
ND1 X:HIS299 4.1 7.5 1.0
OH X:TYR383 4.1 7.7 1.0
CG X:HIS299 4.1 2.0 1.0
CG X:GLU318 4.2 4.1 1.0
CG X:HIS295 4.2 7.7 1.0
ND1 X:HIS295 4.2 5.8 1.0
OE2 X:GLU271 4.2 8.5 1.0
C17 X:KEL707 4.2 11.9 1.0
CG2 X:THR321 4.3 6.1 1.0
CZ X:TYR383 4.5 6.5 1.0
C8 X:KEL707 4.6 13.2 1.0
C16 X:KEL707 4.7 12.1 1.0
CB X:GLU318 4.7 4.6 1.0
OE1 X:GLU271 4.7 11.2 1.0
CD X:GLU271 4.7 8.6 1.0
CB X:THR321 4.8 5.1 1.0
O X:HOH731 4.8 8.1 1.0
OE2 X:GLU296 4.8 10.9 1.0
CA X:GLU318 4.9 5.9 1.0
OE1 X:GLU296 4.9 15.3 1.0
CD2 X:TYR383 4.9 5.5 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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