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Sodium in PDB 3agh: X-Ray Analysis of Lysozyme in the Presence of 200 Mm Arg

Enzymatic activity of X-Ray Analysis of Lysozyme in the Presence of 200 Mm Arg

All present enzymatic activity of X-Ray Analysis of Lysozyme in the Presence of 200 Mm Arg:
3.2.1.17;

Protein crystallography data

The structure of X-Ray Analysis of Lysozyme in the Presence of 200 Mm Arg, PDB code: 3agh was solved by L.Ito, K.Shiraki, K.Hasegawa, S.Baba, T.Kumasaka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.15 / 1.49
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.299, 78.299, 37.284, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 20.5

Other elements in 3agh:

The structure of X-Ray Analysis of Lysozyme in the Presence of 200 Mm Arg also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the X-Ray Analysis of Lysozyme in the Presence of 200 Mm Arg (pdb code 3agh). 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 X-Ray Analysis of Lysozyme in the Presence of 200 Mm Arg, PDB code: 3agh:

Sodium binding site 1 out of 1 in 3agh

Go back to Sodium Binding Sites List in 3agh
Sodium binding site 1 out of 1 in the X-Ray Analysis of Lysozyme in the Presence of 200 Mm Arg


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of X-Ray Analysis of Lysozyme in the Presence of 200 Mm Arg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na131

b:10.0
occ:1.00
O A:SER60 2.3 8.6 1.0
O A:CYS64 2.4 8.2 1.0
O A:ARG73 2.4 10.8 1.0
O A:HOH197 2.4 10.2 1.0
O A:HOH186 2.5 9.2 1.0
OG A:SER72 2.5 12.3 1.0
CB A:SER72 3.3 12.7 1.0
C A:CYS64 3.5 7.3 1.0
C A:SER60 3.5 8.8 1.0
C A:ARG73 3.5 11.1 1.0
CA A:ASN65 3.9 8.5 1.0
N A:ARG73 3.9 12.6 1.0
CA A:SER60 4.1 7.5 1.0
C A:SER72 4.1 13.3 1.0
N A:ASN65 4.2 7.2 1.0
CB A:SER60 4.3 8.3 1.0
CA A:ARG73 4.3 11.9 1.0
CA A:SER72 4.3 14.2 1.0
N A:ASN74 4.4 9.9 1.0
N A:CYS64 4.4 7.6 1.0
C A:ARG61 4.5 10.9 1.0
CA A:ASN74 4.6 9.3 1.0
O A:ARG61 4.6 12.2 1.0
N A:ARG61 4.6 10.5 1.0
CA A:CYS64 4.6 7.7 1.0
O A:SER72 4.6 13.8 1.0
N A:ASP66 4.6 8.0 1.0
O A:HOH271 4.7 25.3 1.0
OD1 A:ASN65 4.7 11.4 1.0
CB A:ASN74 4.7 9.8 1.0
CL A:CL132 4.7 12.8 1.0
CB A:THR69 4.8 9.2 1.0
N A:TRP62 4.8 10.8 1.0
CA A:ARG61 4.8 10.5 0.7
C A:ASN65 4.9 7.3 1.0
CB A:ASN65 4.9 8.6 1.0

Reference:

L.Ito, K.Shiraki, T.Matsuura, M.Okumura, K.Hasegawa, S.Baba, H.Yamaguchi, T.Kumasaka. High-Resolution X-Ray Analysis Reveals Binding of Arginine to Aromatic Residues of Lysozyme Surface: Implication of Suppression of Protein Aggregation By Arginine Protein Eng.Des.Sel. V. 24 269 2011.
ISSN: ISSN 1741-0126
PubMed: 21084280
DOI: 10.1093/PROTEIN/GZQ101
Page generated: Tue Dec 15 06:02:09 2020

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