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Ytterbium in PDB 6enb: LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide

Enzymatic activity of LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide

All present enzymatic activity of LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide:
3.3.2.6;

Protein crystallography data

The structure of LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide, PDB code: 6enb was solved by H.Srinivas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.01 / 1.84
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 77.443, 87.576, 99.058, 90.00, 90.00, 90.00
R / Rfree (%) 15.5 / 18.6

Other elements in 6enb:

The structure of LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Ytterbium Binding Sites:

The binding sites of Ytterbium atom in the LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide (pdb code 6enb). This binding sites where shown within 5.0 Angstroms radius around Ytterbium atom.
In total 2 binding sites of Ytterbium where determined in the LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide, PDB code: 6enb:
Jump to Ytterbium binding site number: 1; 2;

Ytterbium binding site 1 out of 2 in 6enb

Go back to Ytterbium Binding Sites List in 6enb
Ytterbium binding site 1 out of 2 in the LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide


Mono view


Stereo pair view

A full contact list of Ytterbium with other atoms in the Yb binding site number 1 of LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Yb703

b:22.3
occ:1.00
OXT A:ACT702 2.4 20.1 1.0
OD1 A:ASP481 2.4 17.9 1.0
OD2 A:ASP481 2.4 18.2 1.0
O A:HOH957 2.5 20.6 1.0
O A:HOH1179 2.5 20.7 1.0
O A:ACT702 2.6 24.7 1.0
CG A:ASP481 2.8 19.2 1.0
C A:ACT702 2.8 25.0 1.0
CB A:ASP481 4.3 21.1 1.0
CH3 A:ACT702 4.4 25.1 1.0
OD2 A:ASP482 4.4 23.1 1.0
OD1 A:ASP482 4.4 23.4 1.0
O A:HOH888 4.6 17.3 1.0
CG A:ASP482 4.7 24.5 1.0
CB A:LYS479 4.7 19.8 1.0
O A:HOH1257 4.8 35.4 1.0
CG A:LYS479 4.9 25.8 1.0

Ytterbium binding site 2 out of 2 in 6enb

Go back to Ytterbium Binding Sites List in 6enb
Ytterbium binding site 2 out of 2 in the LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide


Mono view


Stereo pair view

A full contact list of Ytterbium with other atoms in the Yb binding site number 2 of LTA4 Hydrolase (E297Q) Mutant in Complex with Pro-Gly-Pro Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Yb704

b:56.9
occ:0.47
OD1 A:ASP175 2.3 39.2 1.0
O A:HOH1094 3.2 57.7 1.0
CG A:ASP175 3.5 39.7 1.0
OD2 A:ASP175 4.1 47.7 1.0
CB A:ASP175 4.7 26.3 1.0
CA A:ASP175 4.7 24.6 1.0
O A:ASP175 4.7 32.8 1.0
C A:ASP175 5.0 30.7 1.0

Reference:

S.Numao, F.Hasler, C.Laguerre, H.Srinivas, N.Wack, P.Jager, A.Schmid, A.Osmont, P.Rothlisberger, J.Houguenade, C.Bergsdorf, J.Dawson, N.Carte, A.Hofmann, C.Markert, L.Hardaker, A.Billich, R.M.Wolf, C.A.Penno, B.Bollbuck, W.Miltz, T.A.Rohn. Feasibility and Physiological Relevance of Designing Highly Potent Aminopeptidase-Sparing Leukotriene A4 Hydrolase Inhibitors. Sci Rep V. 7 13591 2017.
ISSN: ESSN 2045-2322
PubMed: 29051536
DOI: 10.1038/S41598-017-13490-1
Page generated: Wed Dec 16 02:42:16 2020

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