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Chlorine in PDB 1lpy: Multiple Methionine Substitutions in T4 Lysozyme

Enzymatic activity of Multiple Methionine Substitutions in T4 Lysozyme

All present enzymatic activity of Multiple Methionine Substitutions in T4 Lysozyme:
3.2.1.17;

Protein crystallography data

The structure of Multiple Methionine Substitutions in T4 Lysozyme, PDB code: 1lpy was solved by N.C.Gassner, W.A.Baase, B.H.M.Mooers, R.D.Busam, L.H.Weaver, J.D.Lindstrom, M.L.Quillin, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.65
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 60.220, 60.220, 93.240, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Multiple Methionine Substitutions in T4 Lysozyme (pdb code 1lpy). 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 Multiple Methionine Substitutions in T4 Lysozyme, PDB code: 1lpy:

Chlorine binding site 1 out of 1 in 1lpy

Go back to Chlorine Binding Sites List in 1lpy
Chlorine binding site 1 out of 1 in the Multiple Methionine Substitutions 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 Multiple Methionine Substitutions in T4 Lysozyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl178

b:25.7
occ:0.50
O A:HOH215 2.9 20.0 1.0
O A:HOH200 3.0 30.8 1.0
O A:HOH182 3.1 31.1 1.0
CE1 A:HIS31 3.8 24.6 1.0
CB A:ALA49 4.0 13.2 1.0
NE2 A:HIS31 4.1 23.6 1.0
CA A:ALA49 4.2 20.2 1.0
NE2 A:GLN69 4.3 37.3 1.0
CD2 A:LEU66 4.5 22.7 1.0
O A:ALA49 4.9 20.2 1.0
ND1 A:HIS31 4.9 22.5 1.0

Reference:

N.C.Gassner, W.A.Baase, B.H.Mooers, R.D.Busam, L.H.Weaver, J.D.Lindstrom, M.L.Quillin, B.W.Matthews. Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability. Biophys.Chem. V. 100 325 2003.
ISSN: ISSN 0301-4622
PubMed: 12646375
DOI: 10.1016/S0301-4622(02)00290-9
Page generated: Sat Dec 12 08:41:58 2020

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