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Sodium in PDB 2gep: Sulfite Reductase Hemoprotein, Oxidized, Siroheme Feiii [4FE-4S] +2, Sulfite Complex

Enzymatic activity of Sulfite Reductase Hemoprotein, Oxidized, Siroheme Feiii [4FE-4S] +2, Sulfite Complex

All present enzymatic activity of Sulfite Reductase Hemoprotein, Oxidized, Siroheme Feiii [4FE-4S] +2, Sulfite Complex:
1.8.1.2;

Protein crystallography data

The structure of Sulfite Reductase Hemoprotein, Oxidized, Siroheme Feiii [4FE-4S] +2, Sulfite Complex, PDB code: 2gep was solved by B.R.Crane, E.D.Getzoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 69.800, 77.400, 87.800, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / n/a

Other elements in 2gep:

The structure of Sulfite Reductase Hemoprotein, Oxidized, Siroheme Feiii [4FE-4S] +2, Sulfite Complex also contains other interesting chemical elements:

Iron (Fe) 5 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Sulfite Reductase Hemoprotein, Oxidized, Siroheme Feiii [4FE-4S] +2, Sulfite Complex (pdb code 2gep). 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 Sulfite Reductase Hemoprotein, Oxidized, Siroheme Feiii [4FE-4S] +2, Sulfite Complex, PDB code: 2gep:

Sodium binding site 1 out of 1 in 2gep

Go back to Sodium Binding Sites List in 2gep
Sodium binding site 1 out of 1 in the Sulfite Reductase Hemoprotein, Oxidized, Siroheme Feiii [4FE-4S] +2, Sulfite Complex


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Sulfite Reductase Hemoprotein, Oxidized, Siroheme Feiii [4FE-4S] +2, Sulfite Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na590

b:20.0
occ:1.00
 O A:HOH833 1.9 30.8 1.0
O A:ILE362 2.3 11.0 1.0
OD1 A:ASN397 2.4 10.8 1.0
O A:GLN396 2.7 10.6 1.0
O A:ASN395 2.9 12.7 1.0
C A:GLN396 3.2 11.6 1.0
CG A:ASN397 3.3 8.3 1.0
C A:ILE362 3.4 11.8 1.0
CB A:GLN396 3.6 11.1 1.0
ND2 A:ASN397 3.8 8.3 1.0
N A:ASN397 3.9 12.0 1.0
N A:GLY365 3.9 12.3 1.0
O A:HOH757 3.9 21.7 1.0
CA A:GLN396 3.9 9.7 1.0
C A:ASN395 3.9 8.7 1.0
N A:ILE362 4.0 15.3 1.0
O A:HOH708 4.0 16.9 1.0
O A:HOH777 4.1 18.8 1.0
CA A:ASN397 4.1 11.7 1.0
N A:ASN364 4.2 11.6 1.0
CA A:ILE362 4.2 13.3 1.0
CB A:ASN397 4.3 8.7 1.0
CE1 A:PHE361 4.3 12.5 1.0
N A:GLU363 4.4 12.3 1.0
N A:GLN396 4.4 9.3 1.0
CA A:GLY365 4.4 10.2 1.0
OE1 A:GLN396 4.4 9.9 1.0
CD1 A:PHE361 4.4 13.5 1.0
CA A:GLU363 4.5 13.4 1.0
C A:GLU363 4.6 13.1 1.0
CB A:ILE362 4.6 15.1 1.0
C A:ASN364 4.7 12.9 1.0
CA A:ASN364 4.8 12.5 1.0
CG A:GLN396 4.9 8.6 1.0

Reference:

B.R.Crane, L.M.Siegel, E.D.Getzoff. Probing the Catalytic Mechanism of Sulfite Reductase By X-Ray Crystallography: Structures of the Escherichia Coli Hemoprotein in Complex with Substrates, Inhibitors, Intermediates, and Products. Biochemistry V. 36 12120 1997.
ISSN: ISSN 0006-2960
PubMed: 9315849
DOI: 10.1021/BI971066I
Page generated: Mon Oct 7 02:33:57 2024

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