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Chlorine in PDB 3f8v: Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >His

Enzymatic activity of Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >His

All present enzymatic activity of Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >His:
3.2.1.17;

Protein crystallography data

The structure of Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >His, PDB code: 3f8v was solved by B.H.M.Mooers, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.90 / 1.08
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 60.123, 60.123, 95.445, 90.00, 90.00, 120.00
R / Rfree (%) 13.8 / 16.3

Other elements in 3f8v:

The structure of Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >His also contains other interesting chemical elements:

Potassium (K) 1 atom
Sodium (Na) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >His (pdb code 3f8v). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >His, PDB code: 3f8v:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 3f8v

Go back to Chlorine Binding Sites List in 3f8v
Chlorine binding site 1 out of 2 in the Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >His


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >His within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl168

b:15.6
occ:0.60
 O A:HOH209 3.0 19.9 1.0
N A:ARG145 3.1 9.9 1.0
N A:ASN144 3.3 9.6 1.0
C A:THR142 3.4 9.3 1.0
O A:HOH245 3.5 20.7 0.5
CA A:THR142 3.5 9.6 1.0
CB A:THR142 3.6 10.0 1.0
O A:THR142 3.7 9.8 1.0
CB A:ASN144 3.7 12.4 1.0
N A:PRO143 3.7 9.5 1.0
CB A:ARG145 3.8 11.7 1.0
CA A:ASN144 3.8 10.3 1.0
C A:ASN144 4.0 9.9 1.0
CA A:ARG145 4.1 10.1 1.0
C A:PRO143 4.2 9.6 1.0
CG2 A:THR142 4.3 12.0 1.0
CD A:PRO143 4.3 10.8 1.0
CA A:PRO143 4.6 10.0 1.0
O A:HOH230 4.6 17.2 1.0
CG A:ASN144 4.7 17.0 1.0
OG1 A:THR142 4.8 11.9 1.0
N A:THR142 4.9 9.5 1.0
CG A:PRO143 5.0 11.7 1.0

Chlorine binding site 2 out of 2 in 3f8v

Go back to Chlorine Binding Sites List in 3f8v
Chlorine binding site 2 out of 2 in the Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >His


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >His within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl173

b:21.2
occ:0.50
 O A:HOH215 2.9 13.8 1.0
N A:SER136 3.9 10.5 1.0
C A:LYS135 4.0 11.7 1.0
OD1 A:ASN140 4.0 13.5 1.0
CA A:LYS135 4.2 12.2 1.0
O A:LYS135 4.4 12.8 1.0
CA A:SER136 4.6 9.9 1.0
C A:SER136 4.7 9.9 1.0
CB A:LYS135 4.7 14.3 1.0
O A:SER136 4.8 10.2 1.0
O A:HOH282 4.9 19.9 1.0

Reference:

B.H.Mooers, D.E.Tronrud, B.W.Matthews. Evaluation at Atomic Resolution of the Role of Strain in Destabilizing the Temperature-Sensitive T4 Lysozyme Mutant Arg 96 --> His. Protein Sci. V. 18 863 2009.
ISSN: ISSN 0961-8368
PubMed: 19384984
DOI: 10.1002/PRO.93
Page generated: Fri Jul 11 05:01:05 2025

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