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Chlorine in PDB 217l: Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme

Enzymatic activity of Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme

All present enzymatic activity of Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme:
3.2.1.17;

Protein crystallography data

The structure of Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme, PDB code: 217l 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) N/A / 1.70
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 60.900, 60.900, 96.400, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme (pdb code 217l). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme, PDB code: 217l:

Chlorine binding site 1 out of 1 in 217l

Go back to Chlorine Binding Sites List in 217l
Chlorine binding site 1 out of 1 in the Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl178

b:26.1
occ:0.50
O A:HOH182 2.9 21.6 1.0
O A:HOH246 3.3 49.2 1.0
CE1 A:HIS31 3.5 10.3 1.0
O A:HOH215 3.5 12.9 1.0
NE2 A:HIS31 3.7 13.1 1.0
O A:HOH200 3.9 25.7 1.0
NE2 A:GLN69 4.1 9.9 1.0
O A:HOH202 4.3 41.1 1.0
ND1 A:HIS31 4.6 12.3 1.0
CB A:ALA49 4.7 10.5 1.0
CD2 A:LEU66 4.7 15.6 1.0
OD1 A:ASP70 4.7 11.4 1.0
CD2 A:HIS31 5.0 14.7 1.0

Reference:

M.Blaber, X.J.Zhang, B.W.Matthews. Structural Basis of Amino Acid Alpha Helix Propensity. Science V. 260 1637 1993.
ISSN: ISSN 0036-8075
PubMed: 8503008
Page generated: Sat Jul 20 04:55:29 2024

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