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Sodium in PDB 1eq4: Crystal Structures of Salt Bridge Mutants of Human Lysozyme

Enzymatic activity of Crystal Structures of Salt Bridge Mutants of Human Lysozyme

All present enzymatic activity of Crystal Structures of Salt Bridge Mutants of Human Lysozyme:
3.2.1.17;

Protein crystallography data

The structure of Crystal Structures of Salt Bridge Mutants of Human Lysozyme, PDB code: 1eq4 was solved by K.Takano, K.Tsuchimori, Y.Yamagata, K.Yutani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.230, 61.330, 32.770, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / n/a

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structures of Salt Bridge Mutants of Human Lysozyme (pdb code 1eq4). 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 Structures of Salt Bridge Mutants of Human Lysozyme, PDB code: 1eq4:

Sodium binding site 1 out of 1 in 1eq4

Go back to Sodium Binding Sites List in 1eq4
Sodium binding site 1 out of 1 in the Crystal Structures of Salt Bridge Mutants of Human Lysozyme


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structures of Salt Bridge Mutants of Human Lysozyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na601

b:12.0
occ:1.00
O A:SER61 2.1 11.5 1.0
O A:CYS65 2.3 6.3 1.0
O A:HOH195 2.3 9.7 1.0
O A:VAL74 2.3 8.7 1.0
O A:HOH357 2.4 11.7 1.0
CB A:ALA73 3.2 12.1 1.0
C A:CYS65 3.3 6.4 1.0
C A:SER61 3.3 9.9 1.0
C A:VAL74 3.4 9.0 1.0
N A:VAL74 3.7 12.2 1.0
CA A:ASN66 3.8 5.3 1.0
N A:ASN66 3.9 7.5 1.0
C A:ALA73 4.1 13.2 1.0
O A:ARG62 4.1 14.1 1.0
CA A:SER61 4.1 7.9 1.0
C A:ARG62 4.1 13.2 1.0
N A:CYS65 4.2 7.2 1.0
CA A:VAL74 4.2 10.4 1.0
CA A:ALA73 4.2 12.3 1.0
N A:ASN75 4.3 8.2 1.0
N A:ARG62 4.3 10.5 1.0
CA A:CYS65 4.4 7.2 1.0
CB A:SER61 4.4 6.8 1.0
CA A:ARG62 4.4 11.5 1.0
CA A:ASN75 4.5 9.0 1.0
N A:TYR63 4.5 13.5 1.0
O A:HOH150 4.6 12.2 1.0
OD1 A:ASN66 4.6 10.0 1.0
CB A:ASN66 4.6 5.7 1.0
CB A:ASN75 4.7 8.1 1.0
N A:ASP67 4.7 4.7 1.0
C A:ASN66 4.8 5.0 1.0
O A:ALA73 4.8 12.9 1.0
N A:TRP64 4.8 10.2 1.0
C A:TYR63 4.9 12.1 1.0
O A:HOH182 4.9 18.7 1.0
CA A:TYR63 5.0 15.3 1.0

Reference:

K.Takano, K.Tsuchimori, Y.Yamagata, K.Yutani. Contribution of Salt Bridges Near the Surface of A Protein to the Conformational Stability. Biochemistry V. 39 12375 2000.
ISSN: ISSN 0006-2960
PubMed: 11015217
DOI: 10.1021/BI000849S
Page generated: Tue Dec 15 05:23:34 2020

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