Sodium in PDB 1ckd: T43V Mutant Human Lysozyme

All present enzymatic activity of T43V Mutant Human Lysozyme:
3.2.1.17;

The structure of T43V Mutant Human Lysozyme, PDB code: 1ckd was solved by K.Takano, Y.Yamagata, J.Funahashi, 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 (°)	56.640, 61.040, 33.910, 90.00, 90.00, 90.00
R / Rfree (%)	15.1 / n/a

The binding sites of Sodium atom in the T43V Mutant Human Lysozyme (pdb code 1ckd). 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 T43V Mutant Human Lysozyme, PDB code: 1ckd:

Sodium binding site 1 out of 1 in the T43V Mutant Human Lysozyme


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of T43V Mutant Human Lysozyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Na601 b:24.2 occ:1.00 O A:SER61 2.1 10.8 1.0 O A:CYS65 2.3 8.8 1.0 O A:VAL74 2.5 14.8 1.0 CB A:ALA73 3.2 16.5 1.0 C A:SER61 3.3 11.1 1.0 C A:CYS65 3.3 7.4 1.0 C A:VAL74 3.5 14.0 1.0 CA A:ASN66 3.7 7.1 1.0 N A:VAL74 3.8 14.7 1.0 N A:ASN66 3.9 8.3 1.0 C A:ALA73 4.1 16.5 1.0 CA A:SER61 4.1 9.2 1.0 C A:ARG62 4.1 12.8 1.0 O A:ARG62 4.2 13.7 1.0 N A:ARG62 4.2 11.5 1.0 N A:CYS65 4.2 8.1 1.0 CA A:ALA73 4.2 16.8 1.0 CA A:VAL74 4.3 15.1 1.0 CA A:ARG62 4.3 12.6 1.0 N A:ASN75 4.3 12.9 1.0 CA A:CYS65 4.4 7.3 1.0 CA A:ASN75 4.4 12.6 1.0 OD1 A:ASN66 4.5 12.8 1.0 CB A:ASN66 4.5 8.4 1.0 N A:TYR63 4.5 12.5 1.0 CB A:SER61 4.5 6.1 1.0 N A:ASP67 4.7 7.5 1.0 CB A:ASN75 4.7 12.2 1.0 C A:ASN66 4.7 7.4 1.0 O A:ALA73 4.8 15.6 1.0 N A:TRP64 4.9 10.4 1.0 C A:TYR63 4.9 12.5 1.0

K.Takano, Y.Yamagata, J.Funahashi, Y.Hioki, S.Kuramitsu, K.Yutani. Contribution of Intra- and Intermolecular Hydrogen Bonds to the Conformational Stability of Human Lysozyme(,). Biochemistry V. 38 12698 1999.
ISSN: ISSN 0006-2960
PubMed: 10504240
DOI: 10.1021/BI9910169