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Sodium in PDB 3ao0: Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (S)-2-Amino-1-Propanol

Enzymatic activity of Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (S)-2-Amino-1-Propanol

All present enzymatic activity of Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (S)-2-Amino-1-Propanol:
4.3.1.7;

Protein crystallography data

The structure of Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (S)-2-Amino-1-Propanol, PDB code: 3ao0 was solved by N.Shibata, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.00 / 2.25
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 243.850, 243.850, 76.806, 90.00, 90.00, 120.00
R / Rfree (%) 23.5 / 25.7

Other elements in 3ao0:

The structure of Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (S)-2-Amino-1-Propanol also contains other interesting chemical elements:

Cobalt (Co) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (S)-2-Amino-1-Propanol (pdb code 3ao0). 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 Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (S)-2-Amino-1-Propanol, PDB code: 3ao0:

Sodium binding site 1 out of 1 in 3ao0

Go back to Sodium Binding Sites List in 3ao0
Sodium binding site 1 out of 1 in the Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (S)-2-Amino-1-Propanol


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (S)-2-Amino-1-Propanol within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Na454

b:66.9
occ:1.00
 O C:HOH505 3.7 10.4 1.0
CE2 C:TRP91 4.0 33.6 1.0
NE1 C:TRP91 4.0 35.3 1.0
CZ2 C:TRP91 4.3 33.1 1.0
CD C:GLU95 4.4 38.7 1.0
CB C:GLU95 4.4 33.8 1.0
CD2 C:TRP91 4.4 32.7 1.0
CD1 C:TRP91 4.4 35.0 1.0
OE1 C:GLU95 4.5 38.3 1.0
CG C:GLU95 4.6 36.3 1.0
OE2 C:GLU95 4.6 42.6 1.0
CG C:TRP91 4.6 33.8 1.0
O C:HOH629 4.8 2.0 1.0
CH2 C:TRP91 4.9 32.8 1.0
CE3 C:TRP91 5.0 32.8 1.0

Reference:

N.Shibata, Y.Higuchi, T.Toraya. How Coenzyme B12-Dependent Ethanolamine Ammonia-Lyase Deals with Both Enantiomers of 2-Amino-1-Propanol As Substrates: Structure-Based Rationalization. Biochemistry V. 50 591 2011.
ISSN: ISSN 0006-2960
PubMed: 21142024
DOI: 10.1021/BI101696H
Page generated: Mon Oct 7 05:51:11 2024

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