Chlorine in PDB 7l3i: T4 Lysozyme L99A - Propylbenzene - Rt

Enzymatic activity of T4 Lysozyme L99A - Propylbenzene - Rt

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

Protein crystallography data

The structure of T4 Lysozyme L99A - Propylbenzene - Rt, PDB code: 7l3i 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) 35.77 / 1.46
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 60.977, 60.977, 97.268, 90, 90, 120
R / Rfree (%) 14.8 / 16.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the T4 Lysozyme L99A - Propylbenzene - Rt (pdb code 7l3i). 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 - Propylbenzene - Rt, PDB code: 7l3i:

Chlorine binding site 1 out of 1 in 7l3i

Go back to Chlorine Binding Sites List in 7l3i
Chlorine binding site 1 out of 1 in the T4 Lysozyme L99A - Propylbenzene - 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 - Propylbenzene - Rt within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl202

b:25.8
occ:1.00
O A:HOH424 3.0 29.3 1.0
N A:ARG145 3.3 12.7 1.0
N A:ASN144 3.3 13.6 1.0
O A:HOH406 3.4 46.6 1.0
C A:THR142 3.5 13.9 1.0
CA A:THR142 3.5 15.0 1.0
CB A:THR142 3.7 14.6 1.0
CB A:ASN144 3.7 17.5 1.0
N A:PRO143 3.8 13.4 1.0
O A:THR142 3.8 15.5 1.0
CA A:ASN144 3.8 14.3 1.0
CB A:ARG145 4.0 17.0 1.0
C A:ASN144 4.0 13.1 1.0
CD A:PRO143 4.2 15.1 1.0
CA A:ARG145 4.3 13.7 1.0
C A:PRO143 4.3 12.8 1.0
CG2 A:THR142 4.4 17.3 1.0
CA A:PRO143 4.6 13.7 1.0
CG A:ASN144 4.6 23.8 1.0
O A:HOH313 4.7 31.0 1.0
OG1 A:THR142 4.8 16.5 1.0
N A:THR142 5.0 14.3 1.0
ND2 A:ASN144 5.0 27.1 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: Fri Nov 5 12:27:14 2021

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