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Zinc in PDB 5ni6: Crystal Structure of Human LTA4H Mutant D375N in Complex with LTA4

Enzymatic activity of Crystal Structure of Human LTA4H Mutant D375N in Complex with LTA4

All present enzymatic activity of Crystal Structure of Human LTA4H Mutant D375N in Complex with LTA4:
3.3.2.6;

Protein crystallography data

The structure of Crystal Structure of Human LTA4H Mutant D375N in Complex with LTA4, PDB code: 5ni6 was solved by A.Stsiapanava, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.23 / 1.54
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 78.130, 87.450, 99.460, 90.00, 90.00, 90.00
R / Rfree (%) 15.8 / 19.1

Other elements in 5ni6:

The structure of Crystal Structure of Human LTA4H Mutant D375N in Complex with LTA4 also contains other interesting chemical elements:

Ytterbium (Yb) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human LTA4H Mutant D375N in Complex with LTA4 (pdb code 5ni6). 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 Crystal Structure of Human LTA4H Mutant D375N in Complex with LTA4, PDB code: 5ni6:

Zinc binding site 1 out of 1 in 5ni6

Go back to Zinc Binding Sites List in 5ni6
Zinc binding site 1 out of 1 in the Crystal Structure of Human LTA4H Mutant D375N in Complex with LTA4


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human LTA4H Mutant D375N in Complex with LTA4 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:19.8
occ:1.00
 O A:ACY706 1.9 27.3 0.3
OE1 A:GLU318 2.0 20.8 1.0
NE2 A:HIS299 2.1 16.8 1.0
NE2 A:HIS295 2.1 19.1 1.0
OAT A:DJ3705 2.2 29.6 0.2
OXT A:ACY706 2.3 27.1 0.3
C A:ACY706 2.4 30.6 0.3
OAT A:DJ3705 2.4 30.4 0.5
O A:HOH801 2.6 32.0 0.7
CD A:GLU318 2.7 27.0 1.0
OE2 A:GLU318 2.8 28.9 1.0
CE1 A:HIS299 3.0 16.5 1.0
CD2 A:HIS299 3.1 15.2 1.0
CE1 A:HIS295 3.1 18.8 1.0
HE2 A:TYR383 3.1 34.5 1.0
CD2 A:HIS295 3.1 17.7 1.0
HE1 A:HIS299 3.2 19.8 1.0
HD2 A:HIS299 3.2 18.2 1.0
HE1 A:HIS295 3.2 22.6 1.0
HD2 A:HIS295 3.3 21.3 1.0
CAV A:DJ3705 3.4 30.6 0.2
HH A:TYR383 3.5 36.3 1.0
CAW A:DJ3705 3.5 31.9 0.2
O A:HOH861 3.6 33.2 0.9
HA1 A:DJ3705 3.6 36.8 0.2
HAZ A:DJ3705 3.7 43.7 0.2
CAV A:DJ3705 3.8 31.8 0.5
CAW A:DJ3705 3.8 33.6 0.5
HG21 A:THR321 3.8 20.6 1.0
CE2 A:TYR383 3.8 28.7 1.0
CH3 A:ACY706 3.9 31.9 0.3
HA1 A:DJ3705 4.0 38.1 0.5
CAS A:DJ3705 4.1 36.4 0.2
HA A:GLU318 4.1 22.7 1.0
ND1 A:HIS299 4.1 17.3 1.0
OH A:TYR383 4.2 30.3 1.0
ND1 A:HIS295 4.2 18.5 1.0
HA2 A:DJ3705 4.2 38.4 0.2
CG A:HIS299 4.2 16.3 1.0
OE1 A:GLU271 4.2 17.5 1.0
CG A:HIS295 4.2 17.2 1.0
OAB A:DJ3705 4.2 32.7 0.2
HAG A:DJ3705 4.2 44.5 0.2
CG A:GLU318 4.2 20.4 1.0
H2 A:ACY706 4.3 38.4 0.3
HAZ A:DJ3705 4.3 45.6 0.5
HA2 A:DJ3705 4.3 40.3 0.5
H1 A:ACY706 4.4 38.4 0.3
H3 A:ACY706 4.4 38.4 0.3
HAG A:DJ3705 4.4 44.9 0.5
CZ A:TYR383 4.4 28.7 1.0
HB A:THR321 4.4 22.5 1.0
HA0 A:DJ3705 4.4 43.7 0.2
CAS A:DJ3705 4.5 38.0 0.5
HA0 A:DJ3705 4.5 45.6 0.5
HG3 A:GLU318 4.6 24.4 1.0
CG2 A:THR321 4.6 17.2 1.0
CAK A:DJ3705 4.6 33.7 0.2
HB3 A:GLU318 4.6 24.9 1.0
HG22 A:THR321 4.6 20.6 1.0
O A:HOH914 4.7 23.7 1.0
CAG A:DJ3705 4.7 37.1 0.2
HG2 A:GLU318 4.8 24.4 1.0
CD A:GLU271 4.8 18.6 1.0
CD2 A:TYR383 4.8 25.2 1.0
OE2 A:GLU271 4.8 20.5 1.0
HD2 A:TYR383 4.8 30.3 1.0
CB A:GLU318 4.8 20.7 1.0
OE2 A:GLU296 4.9 22.9 1.0
CAK A:DJ3705 4.9 33.2 0.5
CA A:GLU318 4.9 18.9 1.0
HD1 A:HIS299 4.9 20.8 1.0
OE1 A:GLU296 4.9 23.9 1.0
HD1 A:HIS295 4.9 22.2 1.0
CB A:THR321 5.0 18.8 1.0

Reference:

A.Stsiapanava, B.Samuelsson, J.Z.Haeggstrom. Capturing LTA4 Hydrolase in Action: Insights to the Chemistry and Dynamics of Chemotactic LTB4 Synthesis. Proc. Natl. Acad. Sci. V. 114 9689 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28827365
DOI: 10.1073/PNAS.1710850114
Page generated: Sun Oct 27 22:51:41 2024

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