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Sodium in PDB 4htr: N149W Variant of Sirhp Bound to Sulfite

Enzymatic activity of N149W Variant of Sirhp Bound to Sulfite

All present enzymatic activity of N149W Variant of Sirhp Bound to Sulfite:
1.8.1.2;

Protein crystallography data

The structure of N149W Variant of Sirhp Bound to Sulfite, PDB code: 4htr was solved by K.W.Smith, M.E.Stroupe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.07 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 66.458, 76.247, 81.382, 90.00, 90.00, 90.00
R / Rfree (%) 16 / 18.4

Other elements in 4htr:

The structure of N149W Variant of Sirhp Bound to Sulfite also contains other interesting chemical elements:

Iron (Fe) 5 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the N149W Variant of Sirhp Bound to Sulfite (pdb code 4htr). 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 N149W Variant of Sirhp Bound to Sulfite, PDB code: 4htr:

Sodium binding site 1 out of 1 in 4htr

Go back to Sodium Binding Sites List in 4htr
Sodium binding site 1 out of 1 in the N149W Variant of Sirhp Bound to Sulfite


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of N149W Variant of Sirhp Bound to Sulfite within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na602

b:12.2
occ:1.00
OD1 A:ASN397 2.6 7.4 1.0
O A:ILE362 2.7 8.2 1.0
O A:ASN395 2.7 8.2 1.0
O A:HOH760 3.1 12.7 0.9
O A:HOH738 3.3 11.3 0.9
O A:GLN396 3.4 7.6 1.0
CG A:ASN397 3.4 7.9 1.0
O A:HOH798 3.5 12.1 0.9
C A:GLN396 3.7 7.2 1.0
C A:ILE362 3.8 7.4 1.0
CE1 A:PHE361 3.8 9.8 1.0
ND2 A:ASN397 3.8 6.0 1.0
CB A:GLN396 3.8 7.1 1.0
C A:ASN395 3.9 7.1 1.0
CD1 A:PHE361 4.1 7.2 1.0
N A:ASN364 4.2 7.1 1.0
CA A:GLN396 4.2 7.0 1.0
N A:GLY365 4.2 7.7 1.0
N A:ASN397 4.2 7.5 1.0
OE1 A:GLN396 4.3 8.9 1.0
N A:ILE362 4.3 7.8 1.0
CZ A:PHE361 4.5 9.8 1.0
N A:GLN396 4.5 6.0 1.0
CA A:GLU363 4.5 7.9 1.0
N A:GLU363 4.6 7.7 1.0
CA A:ILE362 4.6 7.6 1.0
CA A:ASN397 4.6 6.3 1.0
CB A:ASN397 4.6 5.8 1.0
C A:GLU363 4.7 9.8 1.0
CA A:ASN364 4.8 8.5 1.0
C A:ASN364 4.9 8.7 1.0
CG A:GLN396 4.9 8.2 1.0
CA A:GLY365 4.9 8.3 1.0

Reference:

K.W.Smith, M.E.Stroupe. Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer. Biochemistry V. 51 9857 2012.
ISSN: ISSN 0006-2960
PubMed: 23153334
DOI: 10.1021/BI300947A
Page generated: Tue Dec 15 06:43:48 2020

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