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Sodium in PDB 3b72: Crystal Structure of Lysozyme Folded in Sds and 2-Methyl-2,4- Pentanediol

Enzymatic activity of Crystal Structure of Lysozyme Folded in Sds and 2-Methyl-2,4- Pentanediol

All present enzymatic activity of Crystal Structure of Lysozyme Folded in Sds and 2-Methyl-2,4- Pentanediol:
3.2.1.17;

Protein crystallography data

The structure of Crystal Structure of Lysozyme Folded in Sds and 2-Methyl-2,4- Pentanediol, PDB code: 3b72 was solved by C.Michaux, J.Pouyez, J.Wouters, G.G.Prive, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.50
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 77.900, 77.900, 37.530, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 24.1

Other elements in 3b72:

The structure of Crystal Structure of Lysozyme Folded in Sds and 2-Methyl-2,4- Pentanediol also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Lysozyme Folded in Sds and 2-Methyl-2,4- Pentanediol (pdb code 3b72). 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 Crystal Structure of Lysozyme Folded in Sds and 2-Methyl-2,4- Pentanediol, PDB code: 3b72:

Sodium binding site 1 out of 1 in 3b72

Go back to Sodium Binding Sites List in 3b72
Sodium binding site 1 out of 1 in the Crystal Structure of Lysozyme Folded in Sds and 2-Methyl-2,4- Pentanediol


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Lysozyme Folded in Sds and 2-Methyl-2,4- Pentanediol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na4

b:22.6
occ:1.00
 O A:SER1060 2.2 15.6 1.0
O A:HOH1245 2.4 14.8 1.0
OG A:SER1072 2.4 23.6 1.0
O A:ARG1073 2.4 27.1 1.0
O A:CYS1064 2.6 10.8 1.0
CB A:SER1072 3.0 26.4 1.0
C A:SER1060 3.4 10.6 1.0
C A:ARG1073 3.5 22.0 1.0
C A:CYS1064 3.7 11.1 1.0
N A:ARG1073 3.9 24.4 1.0
CA A:ASN1065 4.0 8.7 1.0
C A:SER1072 4.1 33.4 1.0
CA A:SER1060 4.1 6.3 1.0
CA A:SER1072 4.1 26.9 1.0
O A:ARG1061 4.2 24.4 1.0
N A:ASN1065 4.3 8.5 1.0
CB A:SER1060 4.3 7.2 1.0
CA A:ARG1073 4.3 18.6 1.0
C A:ARG1061 4.3 21.2 1.0
N A:ASN1074 4.3 15.5 1.0
N A:ARG1061 4.4 11.8 1.0
O A:HOH1244 4.5 13.6 1.0
CA A:ARG1061 4.5 16.7 1.0
CB A:THR1069 4.6 10.7 1.0
N A:CYS1064 4.6 13.0 1.0
CA A:ASN1074 4.7 12.2 1.0
N A:ASP1066 4.7 7.8 1.0
O A:SER1072 4.7 26.0 1.0
OD1 A:ASN1065 4.8 16.0 1.0
CA A:CYS1064 4.8 10.9 1.0
O A:THR1069 4.8 21.3 1.0
C A:ASN1065 4.9 8.2 1.0
N A:TRP1062 4.9 13.4 1.0
CB A:ASN1074 4.9 13.5 1.0
CB A:ASN1065 4.9 13.4 1.0

Reference:

C.Michaux, J.Pouyez, J.Wouters, G.G.Prive. Protecting Role of Cosolvents in Protein Denaturation By Sds: A Structural Study. Bmc Struct.Biol. V. 8 29 2008.
ISSN: ESSN 1472-6807
PubMed: 18522744
DOI: 10.1186/1472-6807-8-29
Page generated: Mon Oct 7 06:00:04 2024

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