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Sodium in PDB 8elm: Apo Human Biliverdin Reductase Beta (293K)

Enzymatic activity of Apo Human Biliverdin Reductase Beta (293K)

All present enzymatic activity of Apo Human Biliverdin Reductase Beta (293K):
1.3.1.24; 1.5.1.30;

Protein crystallography data

The structure of Apo Human Biliverdin Reductase Beta (293K), PDB code: 8elm was solved by M.J.Mcleod, E.Z.Eisenmesser, E.Lee, R.E.Thorne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.50 / 2.19
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.591, 47.309, 101.075, 90, 90, 90
R / Rfree (%) 17.5 / 22.6

Sodium Binding Sites:

The binding sites of Sodium atom in the Apo Human Biliverdin Reductase Beta (293K) (pdb code 8elm). 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 Apo Human Biliverdin Reductase Beta (293K), PDB code: 8elm:

Sodium binding site 1 out of 1 in 8elm

Go back to Sodium Binding Sites List in 8elm
Sodium binding site 1 out of 1 in the Apo Human Biliverdin Reductase Beta (293K)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Apo Human Biliverdin Reductase Beta (293K) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na301

b:33.6
occ:1.00
OG1 A:THR12 3.0 46.2 1.0
N A:ARG35 3.2 33.1 1.0
CG2 A:THR12 3.4 36.8 1.0
NH1 A:ARG39 3.5 33.6 1.0
CB A:THR12 3.8 38.3 1.0
CA A:VAL34 3.8 26.8 1.0
CB A:ARG35 3.9 34.7 1.0
CD A:ARG39 3.9 36.3 1.0
CG A:ARG35 3.9 46.5 1.0
CB A:VAL34 4.0 27.7 1.0
C A:VAL34 4.0 27.2 1.0
CA A:ARG35 4.1 31.3 1.0
CG1 A:VAL34 4.4 27.1 1.0
CZ A:ARG39 4.5 42.2 1.0
N A:ASP36 4.6 29.3 1.0
NE A:ARG39 4.6 37.2 1.0
C A:ARG35 4.9 30.7 1.0
O A:LEU33 4.9 29.2 1.0

Reference:

E.Lee, M.J.Mcleod, J.S.Redzic, B.Marcolin, R.E.Thorne, P.Agarwal, E.Z.Eisenmesser. Identifying Structural and Dynamic Changes During the Biliverdin Reductase B Catalytic Cycle Front Mol Biosci V. 10 2023.
ISSN: ESSN 2296-889X
DOI: 10.3389/FMOLB.2023.1244587
Page generated: Mon Aug 18 14:01:15 2025

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