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Sodium in PDB 9dpu: Bmp-9 G389S Dimer in Acidic pH

Protein crystallography data

The structure of Bmp-9 G389S Dimer in Acidic pH, PDB code: 9dpu was solved by T.A.Schwartze, A.P.Hinck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.66 / 2.10
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 71.589, 71.589, 146.719, 90, 90, 90
R / Rfree (%) 19.2 / 22.4

Other elements in 9dpu:

The structure of Bmp-9 G389S Dimer in Acidic pH also contains other interesting chemical elements:

Chlorine (Cl) 5 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Bmp-9 G389S Dimer in Acidic pH (pdb code 9dpu). 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 Bmp-9 G389S Dimer in Acidic pH, PDB code: 9dpu:

Sodium binding site 1 out of 1 in 9dpu

Go back to Sodium Binding Sites List in 9dpu
Sodium binding site 1 out of 1 in the Bmp-9 G389S Dimer in Acidic pH


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Bmp-9 G389S Dimer in Acidic pH within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na506

b:57.6
occ:0.99
OG1 A:THR386 2.5 81.8 1.0
H A:THR386 2.6 66.9 1.0
HA A:PHE384 2.9 61.7 1.0
HD2 A:PRO385 3.1 71.7 1.0
HG3 A:LYS387 3.3 97.8 1.0
HG23 A:THR386 3.3 100.9 1.0
N A:THR386 3.4 55.6 1.0
HB3 A:PHE384 3.5 63.3 1.0
O A:HOH700 3.5 68.7 0.9
HE3 A:LYS387 3.5 176.1 1.0
CA A:PHE384 3.6 51.3 1.0
C A:PHE384 3.6 53.6 1.0
CB A:THR386 3.6 69.3 1.0
N A:PRO385 3.6 45.6 1.0
H A:LYS387 3.7 90.2 1.0
CD A:PRO385 3.8 59.7 1.0
CG2 A:THR386 3.8 84.0 1.0
HD1 A:PHE384 3.9 80.0 1.0
HG2 A:PRO385 4.0 62.6 1.0
HG21 A:THR386 4.0 100.9 1.0
CB A:PHE384 4.0 52.7 1.0
CA A:THR386 4.0 88.6 1.0
O A:PHE384 4.2 57.4 1.0
CG A:LYS387 4.2 81.4 1.0
N A:LYS387 4.3 75.1 1.0
CE A:LYS387 4.4 146.7 1.0
HD2 A:LYS387 4.4 175.1 1.0
HB A:THR386 4.4 83.3 1.0
CG A:PRO385 4.4 52.0 1.0
C A:PRO385 4.4 45.8 1.0
CD A:LYS387 4.6 145.8 1.0
HD3 A:PRO385 4.6 71.7 1.0
CA A:PRO385 4.6 44.8 1.0
C A:THR386 4.7 67.4 1.0
CD1 A:PHE384 4.7 66.6 1.0
O A:LYS383 4.7 58.7 1.0
HG22 A:THR386 4.7 100.9 1.0
HB2 A:LYS387 4.7 83.1 1.0
HB2 A:PHE384 4.8 63.3 1.0
HG2 A:LYS387 4.8 97.8 1.0
N A:PHE384 4.8 52.5 1.0
CG A:PHE384 4.9 72.3 1.0
HA A:THR386 4.9 106.4 1.0
HZ1 A:LYS387 4.9 132.7 1.0
CB A:LYS387 5.0 69.2 1.0
HE2 A:LYS387 5.0 176.1 1.0

Reference:

T.A.Schwartze, S.A.Morosky, T.L.Rosato, A.Henrickson, G.Lin, C.S.Hinck, A.B.Taylor, S.K.Olsen, G.Calero, B.Demeler, B.L.Roman, A.P.Hinck. Molecular Basis of Interchain Disulfide Bond Formation in Bmp-9 and Bmp-10. J.Mol.Biol. V. 437 68935 2025.
ISSN: ESSN 1089-8638
PubMed: 39793884
DOI: 10.1016/J.JMB.2025.168935
Page generated: Mon Aug 18 16:45:45 2025

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