Sodium in PDB 1ip3: G68A Human Lysozyme

All present enzymatic activity of G68A Human Lysozyme:
3.2.1.17;

The structure of G68A Human Lysozyme, PDB code: 1ip3 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 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	42.245, 64.321, 111.120, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / n/a

The binding sites of Sodium atom in the G68A Human Lysozyme (pdb code 1ip3). 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 G68A Human Lysozyme, PDB code: 1ip3:

Sodium binding site 1 out of 1 in the G68A Human Lysozyme


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of G68A Human Lysozyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Na999 b:22.9 occ:1.00 O A:VAL74 2.0 18.3 1.0 O A:CYS65 2.7 2.0 1.0 O A:HOH670 2.7 14.0 1.0 O A:SER61 2.9 2.9 1.0 C A:VAL74 2.9 13.1 1.0 CB A:ALA73 3.3 9.9 1.0 CA A:ASN75 3.4 6.8 1.0 O A:HOH142 3.4 4.8 1.0 N A:VAL74 3.4 9.4 1.0 C A:CYS65 3.5 2.4 1.0 N A:ASN75 3.5 11.5 1.0 CB A:ASN75 3.7 4.4 1.0 O A:ARG62 3.7 9.6 1.0 C A:ALA73 3.8 10.2 1.0 C A:SER61 3.9 3.6 1.0 CA A:ALA73 3.9 9.4 1.0 CA A:VAL74 4.0 11.2 1.0 C A:ARG62 4.0 7.6 1.0 N A:CYS65 4.0 3.4 1.0 N A:ASN66 4.1 2.3 1.0 CA A:ASN66 4.1 2.5 1.0 CA A:CYS65 4.3 2.8 1.0 N A:TRP64 4.4 4.2 1.0 N A:TYR63 4.4 6.6 1.0 C A:TYR63 4.4 5.8 1.0 CG A:ASN75 4.5 4.4 1.0 C A:TRP64 4.5 3.7 1.0 CA A:ARG62 4.5 6.2 1.0 OD1 A:ASN75 4.6 2.3 1.0 N A:ARG62 4.6 3.3 1.0 CA A:TYR63 4.7 8.3 1.0 O A:ALA73 4.7 10.1 1.0 CA A:SER61 4.7 3.3 1.0 O A:TYR63 4.7 4.9 1.0 CB A:ASN66 4.8 4.0 1.0 C A:ASN75 4.8 4.1 1.0 CA A:TRP64 4.9 2.9 1.0

K.Takano, Y.Yamagata, K.Yutani. Role of Amino Acid Residues in Left-Handed Helical Conformation For the Conformational Stability of A Protein. Proteins V. 45 274 2001.
ISSN: ISSN 0887-3585
PubMed: 11599030
DOI: 10.1002/PROT.1147