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Chlorine in PDB 1wqq: Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme

Enzymatic activity of Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme

All present enzymatic activity of Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme:
3.2.1.17;

Protein crystallography data

The structure of Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme, PDB code: 1wqq was solved by Y.Yamagata, M.Kubota, Y.Sumikawa, J.Funahashi, S.Fujii, 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 (°) 56.770, 61.070, 33.880, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / n/a

Other elements in 1wqq:

The structure of Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme also contains other interesting chemical elements:

Sodium (Na) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme (pdb code 1wqq). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme, PDB code: 1wqq:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1wqq

Go back to Chlorine Binding Sites List in 1wqq
Chlorine binding site 1 out of 2 in the Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl132

b:16.2
occ:1.00
O A:HOH234 3.0 33.9 1.0
O A:HOH134 3.3 9.8 1.0
ND2 A:ASN66 3.4 13.6 1.0
CB A:SER80 3.6 17.2 1.0
CA A:SER80 3.6 14.4 1.0
CB A:ASN66 3.9 14.2 1.0
N A:SER80 4.1 14.2 1.0
CG A:ASN66 4.1 15.0 1.0
O A:ASN66 4.2 8.5 1.0
O A:HOH251 4.2 37.1 1.0
OG A:SER80 4.4 15.0 1.0
O A:HOH146 4.4 23.4 1.0
O A:LEU79 4.5 15.4 1.0
C A:LEU79 4.6 15.9 1.0
ND2 A:ASN75 4.6 16.2 1.0
C A:ASN66 4.8 10.6 1.0
CA A:ASN66 4.9 12.2 1.0
O A:HOH172 4.9 24.9 1.0

Chlorine binding site 2 out of 2 in 1wqq

Go back to Chlorine Binding Sites List in 1wqq
Chlorine binding site 2 out of 2 in the Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl133

b:16.3
occ:1.00
O A:HOH165 2.6 31.1 1.0
O A:HOH146 2.7 23.4 1.0
N A:SER80 3.4 14.2 1.0
CB A:SER80 3.9 17.2 1.0
CD2 A:LEU79 4.0 20.5 1.0
CB A:ALA83 4.1 11.9 1.0
CA A:LEU79 4.1 18.7 1.0
CA A:SER80 4.2 14.4 1.0
C A:LEU79 4.2 15.9 1.0
O A:SER80 4.4 13.1 1.0
CB A:LEU79 4.5 19.2 1.0
C A:SER80 4.8 14.2 1.0
CG A:LEU79 4.9 21.1 1.0
O A:HOH234 4.9 33.9 1.0
O A:HOH280 5.0 40.7 1.0
OG A:SER80 5.0 15.0 1.0

Reference:

Y.Yamagata, M.Kubota, Y.Sumikawa, J.Funahashi, K.Takano, S.Fujii, K.Yutani. Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Tyrosine --> Phenylalanine Mutants. Biochemistry V. 37 9355 1998.
ISSN: ISSN 0006-2960
PubMed: 9649316
DOI: 10.1021/BI980431I
Page generated: Sat Dec 12 08:53:59 2020

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