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Sodium in PDB 2ewb: The Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat

Enzymatic activity of The Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat

All present enzymatic activity of The Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat:
3.4.11.1;

Protein crystallography data

The structure of The Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat, PDB code: 2ewb was solved by V.Alterio, C.Pedone, G.De Simone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.85
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 128.940, 128.940, 119.790, 90.00, 90.00, 120.00
R / Rfree (%) 15.6 / 17.7

Other elements in 2ewb:

The structure of The Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the The Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat (pdb code 2ewb). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the The Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat, PDB code: 2ewb:

Sodium binding site 1 out of 1 in 2ewb

Go back to Sodium Binding Sites List in 2ewb
Sodium binding site 1 out of 1 in the The Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of The Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na490

b:5.5
occ:1.00
 O A:ARG271 2.6 9.9 1.0
O A:THR173 2.6 8.4 1.0
O A:LEU170 2.7 9.0 1.0
O A:HOH2063 2.7 9.8 1.0
O A:MET171 2.7 8.1 1.0
C A:MET171 3.3 8.2 1.0
SD A:MET274 3.5 8.2 1.0
C A:ARG271 3.5 8.4 1.0
CA A:MET171 3.7 8.1 1.0
C A:THR173 3.7 9.3 1.0
C A:LEU170 3.8 9.0 1.0
CG A:MET178 3.9 8.9 1.0
CB A:MET178 3.9 8.3 1.0
N A:THR173 4.1 9.2 1.0
CB A:ARG271 4.1 9.5 1.0
N A:MET171 4.2 8.0 1.0
CG A:MET274 4.2 7.3 1.0
CE A:MET274 4.3 7.9 1.0
CG A:ARG271 4.3 7.9 1.0
N A:GLU172 4.3 7.6 1.0
CA A:THR173 4.3 8.9 1.0
CA A:ARG271 4.3 9.1 1.0
C A:GLU172 4.3 8.2 1.0
N A:ALA272 4.4 8.2 1.0
CA A:ALA272 4.5 7.4 1.0
CB A:THR173 4.5 9.6 1.0
O A:THR253 4.7 7.7 1.0
CD A:ARG271 4.7 9.3 1.0
O A:GLU172 4.7 8.5 1.0
C A:PRO174 4.8 8.3 1.0
CA A:GLU172 4.8 7.7 1.0
N A:ALA175 4.8 7.7 1.0
N A:PRO174 4.9 8.9 1.0
O A:PRO174 5.0 9.0 1.0

Reference:

M.Cappiello, V.Alterio, P.Amodeo, A.Del Corso, A.Scaloni, C.Pedone, R.Moschini, G.M.De Donatis, G.De Simone, U.Mura. Metal Ion Substitution in the Catalytic Site Greatly Affects the Binding of Sulfhydryl-Containing Compounds to Leucyl Aminopeptidase. Biochemistry V. 45 3226 2006.
ISSN: ISSN 0006-2960
PubMed: 16519517
DOI: 10.1021/BI052069V
Page generated: Mon Oct 7 02:25:06 2024

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