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Sodium in PDB 2d4f: The Crystal Structure of Human BETA2-Microglobulin

Protein crystallography data

The structure of The Crystal Structure of Human BETA2-Microglobulin, PDB code: 2d4f was solved by K.Iwata, T.Matsuura, A.Nakagawa, Y.Goto, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.45 / 1.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 77.649, 28.869, 54.756, 90.00, 121.66, 90.00
R / Rfree (%) 20.7 / 23.3

Sodium Binding Sites:

The binding sites of Sodium atom in the The Crystal Structure of Human BETA2-Microglobulin (pdb code 2d4f). 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 The Crystal Structure of Human BETA2-Microglobulin, PDB code: 2d4f:

Sodium binding site 1 out of 1 in 2d4f

Go back to Sodium Binding Sites List in 2d4f
Sodium binding site 1 out of 1 in the The Crystal Structure of Human BETA2-Microglobulin


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of The Crystal Structure of Human BETA2-Microglobulin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na101

b:16.7
occ:1.00
O A:LEU87 2.2 11.6 1.0
O A:HOH106 2.3 14.8 1.0
O A:HOH126 2.3 16.0 1.0
O A:HOH118 2.3 18.4 1.0
O A:HOH109 2.5 13.8 1.0
O A:HIS84 2.6 8.8 1.0
C A:LEU87 3.4 11.2 1.0
C A:HIS84 3.6 8.0 1.0
N A:HIS84 4.0 8.5 1.0
CA A:LEU87 4.3 10.4 1.0
N A:LEU87 4.3 8.9 1.0
N A:SER88 4.3 11.8 1.0
CA A:VAL85 4.3 8.9 1.0
N A:VAL85 4.4 8.8 1.0
C A:SER88 4.4 13.0 1.0
O A:SER88 4.4 13.2 1.0
CA A:SER88 4.4 12.7 1.0
CB A:LEU87 4.4 10.3 1.0
CA A:HIS84 4.5 8.1 1.0
C A:VAL85 4.5 9.2 1.0
OD1 A:ASN83 4.5 20.4 1.0
O A:HOH160 4.6 37.9 1.0
O A:VAL85 4.6 9.4 1.0
C A:ASN83 4.9 8.8 1.0
N A:GLN89 4.9 13.2 1.0
CA A:ASN83 5.0 8.9 1.0

Reference:

M.Kihara, E.Chatani, K.Iwata, K.Yamamoto, T.Matsuura, A.Nakagawa, H.Naiki, Y.Goto. Conformation of Amyloid Fibrils of BETA2-Microglobulin Probed By Tryptophan Mutagenesis J.Biol.Chem. V. 281 31061 2006.
ISSN: ISSN 0021-9258
PubMed: 16901902
DOI: 10.1074/JBC.M605358200
Page generated: Mon Oct 7 02:11:03 2024

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