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Chlorine in PDB 3dmv: Free of Ligand Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant

Enzymatic activity of Free of Ligand Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant

All present enzymatic activity of Free of Ligand Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant:
3.2.1.17;

Protein crystallography data

The structure of Free of Ligand Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant, PDB code: 3dmv was solved by L.Liu, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.55 / 1.65
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 59.902, 59.902, 95.307, 90.00, 90.00, 120.00
R / Rfree (%) 18.3 / 21

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Free of Ligand Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant (pdb code 3dmv). 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 Free of Ligand Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant, PDB code: 3dmv:

Chlorine binding site 1 out of 1 in 3dmv

Go back to Chlorine Binding Sites List in 3dmv
Chlorine binding site 1 out of 1 in the Free of Ligand Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Free of Ligand Binding in the Hydrophobic Cavity of T4 Lysozyme L99A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl902

b:46.4
occ:1.00
O A:HOH998 3.2 28.6 1.0
O A:HOH1002 3.3 43.6 1.0
NH1 A:ARG148 3.6 13.1 1.0
ND2 A:ASN144 3.7 17.7 1.0
O A:HOH1134 3.8 41.9 1.0
CB A:ASN144 3.9 11.5 1.0
CG A:ASN144 4.3 13.8 1.0
CZ A:ARG148 4.6 11.7 1.0
NH2 A:ARG148 4.6 11.5 1.0
O A:HOH1052 4.8 14.9 1.0

Reference:

L.Liu, W.A.Baase, B.W.Matthews. Halogenated Benzenes Bound Within A Non-Polar Cavity in T4 Lysozyme Provide Examples of I...S and I...Se Halogen-Bonding. J.Mol.Biol. V. 385 595 2009.
ISSN: ISSN 0022-2836
PubMed: 19014950
DOI: 10.1016/J.JMB.2008.10.086
Page generated: Sat Jul 20 18:22:44 2024

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