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Sodium in PDB 1di4: Role of Amino Acid Residues at Turns in the Conformational Stability and Folding of Human Lysozyme

Enzymatic activity of Role of Amino Acid Residues at Turns in the Conformational Stability and Folding of Human Lysozyme

All present enzymatic activity of Role of Amino Acid Residues at Turns in the Conformational Stability and Folding of Human Lysozyme:
3.2.1.17;

Protein crystallography data

The structure of Role of Amino Acid Residues at Turns in the Conformational Stability and Folding of Human Lysozyme, PDB code: 1di4 was solved by K.Takano, 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 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.800, 59.270, 38.910, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / n/a

Sodium Binding Sites:

The binding sites of Sodium atom in the Role of Amino Acid Residues at Turns in the Conformational Stability and Folding of Human Lysozyme (pdb code 1di4). 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 Role of Amino Acid Residues at Turns in the Conformational Stability and Folding of Human Lysozyme, PDB code: 1di4:

Sodium binding site 1 out of 1 in 1di4

Go back to Sodium Binding Sites List in 1di4
Sodium binding site 1 out of 1 in the Role of Amino Acid Residues at Turns in the Conformational Stability and Folding 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 Role of Amino Acid Residues at Turns in the Conformational Stability and Folding of Human Lysozyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na501

b:18.1
occ:1.00
 O A:VAL74 2.0 29.1 1.0
O A:CYS65 2.2 12.0 1.0
O A:SER61 2.8 12.2 1.0
C A:CYS65 3.2 11.8 1.0
C A:VAL74 3.2 22.4 1.0
O A:ARG62 3.2 12.6 1.0
CB A:ALA73 3.5 14.3 1.0
C A:ARG62 3.6 12.3 1.0
N A:CYS65 3.6 8.0 1.0
N A:VAL74 3.6 20.3 1.0
C A:SER61 3.6 12.7 1.0
C A:TYR63 3.7 10.8 1.0
CA A:ASN75 3.7 14.1 1.0
N A:TRP64 3.8 9.3 1.0
O A:TYR63 3.8 8.9 1.0
O A:HOH317 3.9 26.8 1.0
N A:TYR63 3.9 11.4 1.0
C A:TRP64 3.9 9.1 1.0
N A:ASN75 4.0 19.2 1.0
CA A:ALA73 4.0 17.8 1.0
CA A:CYS65 4.0 9.3 1.0
CA A:TYR63 4.0 14.5 1.0
N A:ASN66 4.0 11.5 1.0
C A:ALA73 4.1 19.9 1.0
CB A:ASN75 4.2 12.2 1.0
CA A:ASN66 4.2 9.9 1.0
CA A:VAL74 4.3 20.8 1.0
CA A:ARG62 4.3 13.6 1.0
N A:ARG62 4.3 12.0 1.0
CA A:TRP64 4.3 8.4 1.0
CA A:SER61 4.5 11.3 1.0
O A:TRP64 4.6 10.1 1.0
OD1 A:ASN75 4.8 7.1 1.0
CB A:VAL74 4.9 20.6 1.0
CB A:ASN66 5.0 12.8 1.0
CG A:ASN75 5.0 9.8 1.0
C A:ASN75 5.0 14.7 1.0

Reference:

K.Takano, Y.Yamagata, K.Yutani. Role of Amino Acid Residues at Turns in the Conformational Stability and Folding of Human Lysozyme. Biochemistry V. 39 8655 2000.
ISSN: ISSN 0006-2960
PubMed: 10913274
DOI: 10.1021/BI9928694
Page generated: Sun Oct 6 18:04:12 2024

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