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Chlorine in PDB 206l: Phage T4 Lysozyme

Enzymatic activity of Phage T4 Lysozyme

All present enzymatic activity of Phage T4 Lysozyme:
3.2.1.17;

Protein crystallography data

The structure of Phage T4 Lysozyme, PDB code: 206l was solved by M.Blaber, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.75
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 61.000, 61.000, 97.000, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Phage T4 Lysozyme (pdb code 206l). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Phage T4 Lysozyme, PDB code: 206l:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 206l

Go back to Chlorine Binding Sites List in 206l
Chlorine binding site 1 out of 2 in the Phage T4 Lysozyme


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Phage T4 Lysozyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl173

b:22.2
occ:1.00
O A:HOH209 3.1 24.9 1.0
N A:ASN144 3.4 5.9 1.0
N A:ARG145 3.4 12.1 1.0
C A:THR142 3.5 13.7 1.0
CA A:THR142 3.5 12.7 1.0
CB A:THR142 3.6 12.1 1.0
CB A:ASN144 3.8 13.0 1.0
N A:PRO143 3.9 19.6 1.0
O A:THR142 3.9 14.4 1.0
CA A:ASN144 3.9 12.4 1.0
CB A:ARG145 4.1 14.6 1.0
CD A:PRO143 4.1 20.0 1.0
C A:ASN144 4.2 25.4 1.0
CG2 A:THR142 4.2 11.3 1.0
C A:PRO143 4.3 9.5 1.0
CA A:ARG145 4.3 7.2 1.0
CA A:PRO143 4.6 13.8 1.0
ND2 A:ASN144 4.7 24.4 1.0
CG A:ASN144 4.7 30.6 1.0
O A:HOH230 4.7 30.5 1.0
OG1 A:THR142 4.8 12.6 1.0
N A:THR142 5.0 10.9 1.0

Chlorine binding site 2 out of 2 in 206l

Go back to Chlorine Binding Sites List in 206l
Chlorine binding site 2 out of 2 in the Phage T4 Lysozyme


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Phage T4 Lysozyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl178

b:29.6
occ:0.50
O A:HOH215 3.1 18.9 1.0
O A:HOH200 3.2 23.8 1.0
O A:HOH182 3.3 23.2 1.0
O A:HOH246 3.8 36.0 1.0
CB A:ALA49 3.9 13.3 1.0
CE1 A:HIS31 4.1 12.1 1.0
NE2 A:HIS31 4.2 13.7 1.0
O A:HOH282 4.3 32.2 1.0
O A:HOH202 4.5 56.7 1.0
CA A:ALA49 4.5 15.3 1.0
NE2 A:GLN69 4.5 16.6 1.0
O A:HOH307 4.6 79.8 1.0
CD2 A:LEU66 4.9 20.3 1.0

Reference:

M.Blaber, J.D.Lindstrom, N.Gassner, J.Xu, D.W.Heinz, B.W.Matthews. Energetic Cost and Structural Consequences of Burying A Hydroxyl Group Within the Core of A Protein Determined From Ala-->Ser and Val-->Thr Substitutions in T4 Lysozyme. Biochemistry V. 32 11363 1993.
ISSN: ISSN 0006-2960
PubMed: 8218201
DOI: 10.1021/BI00093A013
Page generated: Sat Dec 12 08:57:40 2020

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