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Sodium in PDB 2d1e: Crystal Structure of Pcya-Biliverdin Complex

Enzymatic activity of Crystal Structure of Pcya-Biliverdin Complex

All present enzymatic activity of Crystal Structure of Pcya-Biliverdin Complex:
1.3.7.5;

Protein crystallography data

The structure of Crystal Structure of Pcya-Biliverdin Complex, PDB code: 2d1e was solved by Y.Hagiwara, M.Sugishima, Y.Takahashi, K.Fukuyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.67 / 1.51
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 70.826, 94.997, 42.675, 90.00, 90.00, 90.00
R / Rfree (%) 15.7 / 18.3

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Pcya-Biliverdin Complex (pdb code 2d1e). 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 Pcya-Biliverdin Complex, PDB code: 2d1e:

Sodium binding site 1 out of 1 in 2d1e

Go back to Sodium Binding Sites List in 2d1e
Sodium binding site 1 out of 1 in the Crystal Structure of Pcya-Biliverdin Complex


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 Pcya-Biliverdin Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na249

b:32.8
occ:1.00
OE1 A:GLU50 2.2 23.7 0.7
CD A:GLU50 2.9 21.9 0.7
OE2 A:GLU50 3.2 22.0 0.7
OH A:TYR48 3.4 28.7 1.0
NZ A:LYS57 3.7 17.7 0.3
CG A:GLU50 4.1 19.4 0.7
CD A:LYS57 4.1 16.7 0.3
CG A:GLU50 4.4 13.6 0.3
CE A:LYS57 4.5 16.6 0.3
CG2 A:VAL59 4.6 17.6 1.0
CZ A:TYR48 4.7 26.9 1.0
CD A:LYS57 4.7 23.3 0.7
CE A:LYS57 4.7 26.2 0.7
OE1 A:GLU50 4.8 18.8 0.3
CB A:GLU50 4.8 15.7 0.3
CB A:GLU50 4.8 17.3 0.7
CD A:GLU50 4.9 13.6 0.3

Reference:

Y.Hagiwara, M.Sugishima, Y.Takahashi, K.Fukuyama. Crystal Structure of Phycocyanobilin:Ferredoxin Oxidoreductase in Complex with Biliverdin Ixalpha, A Key Enzyme in the Biosynthesis of Phycocyanobilin Proc.Natl.Acad.Sci.Usa V. 103 27 2006.
ISSN: ISSN 0027-8424
PubMed: 16380422
DOI: 10.1073/PNAS.0507266103
Page generated: Mon Oct 7 02:11:03 2024

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