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Zinc in PDB 5ni2: Crystal Structure of Human LTA4H Mutant E271A in Complex with LTA4 (Crystal Form I)

Enzymatic activity of Crystal Structure of Human LTA4H Mutant E271A in Complex with LTA4 (Crystal Form I)

All present enzymatic activity of Crystal Structure of Human LTA4H Mutant E271A in Complex with LTA4 (Crystal Form I):
3.3.2.6;

Protein crystallography data

The structure of Crystal Structure of Human LTA4H Mutant E271A in Complex with LTA4 (Crystal Form I), PDB code: 5ni2 was solved by A.Stsiapanava, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.37 / 1.50
Space group P 21 2 21
Cell size a, b, c (Å), α, β, γ (°) 67.710, 84.610, 133.430, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 19.6

Other elements in 5ni2:

The structure of Crystal Structure of Human LTA4H Mutant E271A in Complex with LTA4 (Crystal Form I) 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 E271A in Complex with LTA4 (Crystal Form I) (pdb code 5ni2). 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 E271A in Complex with LTA4 (Crystal Form I), PDB code: 5ni2:

Zinc binding site 1 out of 1 in 5ni2

Go back to Zinc Binding Sites List in 5ni2
Zinc binding site 1 out of 1 in the Crystal Structure of Human LTA4H Mutant E271A in Complex with LTA4 (Crystal Form I)


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 E271A in Complex with LTA4 (Crystal Form I) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:27.8
occ:0.96
 OE1 A:GLU318 2.0 25.8 1.0
NE2 A:HIS299 2.0 22.8 1.0
NE2 A:HIS295 2.1 29.0 1.0
OAT A:DJ3704 2.1 29.4 0.3
OAT A:DJ3704 2.2 37.0 0.4
OAT A:DJ3704 2.2 37.0 0.3
CD A:GLU318 2.7 27.0 1.0
OE2 A:GLU318 2.7 33.0 1.0
O A:HOH802 2.8 32.5 0.5
CE1 A:HIS299 2.8 26.9 1.0
CAV A:DJ3704 2.9 41.1 0.3
HE1 A:HIS299 2.9 32.3 1.0
HE2 A:TYR383 3.0 28.5 1.0
HA1 A:DJ3704 3.0 49.4 0.3
CD2 A:HIS295 3.1 25.4 1.0
CE1 A:HIS295 3.1 24.9 1.0
CD2 A:HIS299 3.1 26.8 1.0
CAV A:DJ3704 3.2 42.7 0.4
HD2 A:HIS295 3.2 30.4 1.0
HE1 A:HIS295 3.3 29.9 1.0
CAV A:DJ3704 3.3 44.0 0.3
HH A:TYR383 3.3 32.8 1.0
CAW A:DJ3704 3.4 42.2 0.3
HD2 A:HIS299 3.4 32.2 1.0
HA1 A:DJ3704 3.4 51.2 0.4
HAZ A:DJ3704 3.6 43.1 0.3
HA1 A:DJ3704 3.6 52.9 0.3
HG21 A:THR321 3.6 34.9 1.0
CAW A:DJ3704 3.6 42.0 0.4
CAW A:DJ3704 3.7 43.3 0.3
CE2 A:TYR383 3.7 23.8 1.0
HAW A:DJ3704 3.9 44.0 0.3
HA A:GLU318 3.9 30.4 1.0
OH A:TYR383 4.0 27.3 1.0
CAS A:DJ3704 4.0 35.9 0.3
ND1 A:HIS299 4.0 26.1 1.0
CG A:GLU318 4.1 23.9 1.0
HB A:THR321 4.1 31.1 1.0
CG A:HIS299 4.2 24.6 1.0
O A:HOH1192 4.2 32.1 1.0
HAG A:DJ3704 4.2 52.0 0.4
ND1 A:HIS295 4.2 25.9 1.0
CG A:HIS295 4.2 25.6 1.0
HAG A:DJ3704 4.2 52.3 0.3
HAG A:DJ3704 4.2 51.2 0.3
HA2 A:DJ3704 4.2 50.6 0.3
CZ A:TYR383 4.3 26.3 1.0
CAK A:DJ3704 4.3 41.3 0.3
CG2 A:THR321 4.4 29.1 1.0
HA2 A:DJ3704 4.4 52.0 0.3
CAK A:DJ3704 4.4 41.6 0.4
HA2 A:DJ3704 4.4 50.4 0.4
HAZ A:DJ3704 4.4 51.2 0.4
HG3 A:GLU318 4.5 28.8 1.0
CAQ A:DJ3704 4.5 36.7 0.3
HG22 A:THR321 4.5 34.9 1.0
HAZ A:DJ3704 4.5 50.4 0.3
CAK A:DJ3704 4.5 41.5 0.3
CAS A:DJ3704 4.5 42.7 0.4
HB3 A:GLU318 4.5 28.2 1.0
CAS A:DJ3704 4.5 42.0 0.3
HA0 A:DJ3704 4.6 50.4 0.3
O A:HOH908 4.6 29.6 1.0
HA0 A:DJ3704 4.6 51.2 0.4
CD2 A:TYR383 4.7 25.5 1.0
HG2 A:GLU318 4.7 28.8 1.0
CB A:THR321 4.7 25.9 1.0
CB A:GLU318 4.7 23.5 1.0
HD2 A:TYR383 4.7 30.6 1.0
CAG A:DJ3704 4.7 43.3 0.4
HD1 A:HIS299 4.7 31.4 1.0
CA A:GLU318 4.8 25.3 1.0
CAG A:DJ3704 4.8 42.7 0.3
OE1 A:GLU296 4.8 32.5 1.0
CAG A:DJ3704 4.8 43.6 0.3
HA0 A:DJ3704 4.9 43.1 0.3
O A:HOH935 5.0 35.2 1.0
HD1 A:HIS295 5.0 31.1 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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