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Chlorine in PDB 7l3c: T4 Lysozyme L99A - O-Xylene - Rt

Enzymatic activity of T4 Lysozyme L99A - O-Xylene - Rt

All present enzymatic activity of T4 Lysozyme L99A - O-Xylene - Rt:
3.2.1.17;

Protein crystallography data

The structure of T4 Lysozyme L99A - O-Xylene - Rt, PDB code: 7l3c was solved by M.Fischer, S.Y.C.Bradford, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.51 / 1.31
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 61.038, 61.038, 97.896, 90, 90, 120
R / Rfree (%) 15.2 / 17.7

Chlorine Binding Sites:

The binding sites of Chlorine atom in the T4 Lysozyme L99A - O-Xylene - Rt (pdb code 7l3c). 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 T4 Lysozyme L99A - O-Xylene - Rt, PDB code: 7l3c:

Chlorine binding site 1 out of 1 in 7l3c

Go back to Chlorine Binding Sites List in 7l3c
Chlorine binding site 1 out of 1 in the T4 Lysozyme L99A - O-Xylene - Rt


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of T4 Lysozyme L99A - O-Xylene - Rt within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl202

b:22.1
occ:1.00
O A:HOH391 3.1 39.1 1.0
N A:ASN144 3.3 14.0 1.0
N A:ARG145 3.3 14.4 1.0
O A:HOH364 3.4 31.1 0.5
C A:THR142 3.5 13.6 1.0
CA A:THR142 3.6 14.5 1.0
CB A:ASN144 3.7 18.0 1.0
N A:PRO143 3.7 14.0 1.0
CB A:THR142 3.7 15.1 1.0
O A:THR142 3.8 14.2 1.0
CA A:ASN144 3.8 15.4 1.0
CB A:ARG145 4.0 17.0 1.0
C A:ASN144 4.1 13.9 1.0
CD A:PRO143 4.1 15.6 1.0
C A:PRO143 4.3 13.0 1.0
CA A:ARG145 4.3 14.9 1.0
CG2 A:THR142 4.4 16.6 1.0
CA A:PRO143 4.6 13.6 1.0
CG A:ASN144 4.6 23.7 1.0
ND2 A:ASN144 4.8 25.6 1.0
CG A:PRO143 4.8 16.4 1.0
OG1 A:THR142 4.9 16.8 1.0
N A:THR142 5.0 14.6 1.0

Reference:

S.Y.C.Bradford, L.El Khoury, Y.Ge, M.Osato, D.L.Mobley, M.Fischer. Temperature Artifacts in Protein Structures Bias Ligand-Binding Predictions. Chem Sci V. 12 11275 2021.
ISSN: ISSN 2041-6520
PubMed: 34667539
DOI: 10.1039/D1SC02751D
Page generated: Sun Jul 13 03:33:42 2025

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