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Chlorine in PDB 3fa0: 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: 3fa0 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) 28.00 / 1.09
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 60.370, 60.370, 96.570, 90.00, 90.00, 120.00
R / Rfree (%) 15.8 / 18.8

Other elements in 3fa0:

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

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 3fa0). 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: 3fa0:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 3fa0

Go back to Chlorine Binding Sites List in 3fa0
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:Cl173

b:21.4
occ:0.60
 O A:HOH209 2.8 26.1 1.0
N A:ARG145 2.9 12.3 1.0
C A:THR142 3.3 11.9 1.0
N A:ASN144 3.4 12.1 1.0
CB A:THR142 3.4 12.9 1.0
CB A:ARG145 3.4 14.2 1.0
CA A:THR142 3.4 11.9 1.0
O A:THR142 3.5 13.0 1.0
N A:PRO143 3.8 11.8 1.0
CA A:ARG145 3.8 12.3 1.0
CA A:ASN144 3.8 12.6 1.0
CB A:ASN144 3.8 13.9 1.0
C A:ASN144 3.9 11.9 1.0
CG2 A:THR142 4.1 14.5 1.0
C A:PRO143 4.2 12.0 1.0
CD A:PRO143 4.4 13.0 1.0
O A:HOH230 4.5 22.6 1.0
OG1 A:THR142 4.5 14.4 1.0
CA A:PRO143 4.6 11.7 1.0
N A:ALA146 4.8 12.6 1.0
N A:THR142 4.9 12.2 1.0
C A:ARG145 4.9 12.4 1.0
CG A:ARG145 4.9 19.1 1.0
CG A:ASN144 4.9 17.7 1.0
O A:HOH237 5.0 28.0 1.0

Chlorine binding site 2 out of 2 in 3fa0

Go back to Chlorine Binding Sites List in 3fa0
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:Cl178

b:28.8
occ:0.50
 OD1 A:ASN140 2.9 17.9 1.0
O A:ALA134 3.4 15.0 1.0
CG A:ASN140 3.9 15.5 1.0
CA A:LYS135 3.9 15.0 1.0
N A:SER136 4.0 12.9 1.0
ND2 A:ASN140 4.1 16.4 1.0
C A:LYS135 4.3 13.9 1.0
O A:HOH215 4.4 15.3 1.0
C A:ALA134 4.4 14.9 1.0
O A:SER136 4.6 12.1 1.0
N A:LYS135 4.6 13.6 1.0
CB A:LYS135 4.8 16.3 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: Sat Jul 20 19:14:48 2024

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