Chlorine in PDB 2f47: Xray Crystal Structure of T4 Lysozyme Mutant L20/R63A Liganded to Methylguanidinium

All present enzymatic activity of Xray Crystal Structure of T4 Lysozyme Mutant L20/R63A Liganded to Methylguanidinium:
3.2.1.17;

The structure of Xray Crystal Structure of T4 Lysozyme Mutant L20/R63A Liganded to Methylguanidinium, PDB code: 2f47 was solved by M.S.Yousef, N.Bischoff, C.M.Dyer, W.A.Baase, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.70
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	60.685, 60.685, 95.482, 90.00, 90.00, 120.00
R / Rfree (%)	20.6 / 21.7

The binding sites of Chlorine atom in the Xray Crystal Structure of T4 Lysozyme Mutant L20/R63A Liganded to Methylguanidinium (pdb code 2f47). 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 Xray Crystal Structure of T4 Lysozyme Mutant L20/R63A Liganded to Methylguanidinium, PDB code: 2f47:

Chlorine binding site 1 out of 1 in the Xray Crystal Structure of T4 Lysozyme Mutant L20/R63A Liganded to Methylguanidinium


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Xray Crystal Structure of T4 Lysozyme Mutant L20/R63A Liganded to Methylguanidinium within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl600 b:24.2 occ:1.00 O A:HOH918 3.0 17.9 1.0 O A:HOH912 3.2 16.5 1.0 O A:HOH1035 3.2 31.7 1.0 NE2 A:HIS31 3.6 18.0 1.0 CB A:ALA60 3.7 15.7 1.0 O A:HOH1034 4.0 32.6 1.0 CE1 A:HIS31 4.1 13.6 1.0 NE2 A:GLN80 4.3 14.9 1.0 CA A:ALA60 4.4 16.9 1.0 O A:HOH972 4.5 34.2 1.0 CD2 A:LEU77 4.7 18.7 1.0 CD2 A:HIS31 4.7 13.7 1.0 O A:HOH1040 5.0 41.1 1.0

M.S.Yousef, N.Bischoff, C.M.Dyer, W.A.Baase, B.W.Matthews. Guanidinium Derivatives Bind Preferentially and Trigger Long-Distance Conformational Changes in An Engineered T4 Lysozyme. Protein Sci. V. 15 853 2006.
ISSN: ISSN 0961-8368
PubMed: 16600969
DOI: 10.1110/PS.052020606