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Chlorine in PDB 7l38: T4 Lysozyme L99A - Apo - Cryo

Enzymatic activity of T4 Lysozyme L99A - Apo - Cryo

All present enzymatic activity of T4 Lysozyme L99A - Apo - Cryo:
3.2.1.17;

Protein crystallography data

The structure of T4 Lysozyme L99A - Apo - Cryo, PDB code: 7l38 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) 51.82 / 1.33
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 59.835, 59.835, 96.334, 90, 90, 120
R / Rfree (%) 17.8 / 20

Chlorine Binding Sites:

The binding sites of Chlorine atom in the T4 Lysozyme L99A - Apo - Cryo (pdb code 7l38). 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 - Apo - Cryo, PDB code: 7l38:

Chlorine binding site 1 out of 1 in 7l38

Go back to Chlorine Binding Sites List in 7l38
Chlorine binding site 1 out of 1 in the T4 Lysozyme L99A - Apo - Cryo


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 - Apo - Cryo within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl204

b:29.1
occ:1.00
N A:ARG145 3.3 20.4 1.0
N A:ASN144 3.3 20.3 1.0
C A:THR142 3.4 19.4 1.0
CA A:THR142 3.5 20.3 1.0
CB A:THR142 3.7 19.5 1.0
N A:PRO143 3.7 20.4 1.0
CB A:ASN144 3.7 23.3 1.0
O A:THR142 3.8 19.2 1.0
CA A:ASN144 3.8 20.6 1.0
CB A:ARG145 4.0 23.6 1.0
C A:ASN144 4.0 20.4 1.0
CD A:PRO143 4.1 21.4 1.0
C A:PRO143 4.2 20.2 1.0
CA A:ARG145 4.3 21.3 1.0
CG2 A:THR142 4.4 21.6 1.0
CA A:PRO143 4.5 21.3 1.0
CG A:ASN144 4.7 28.1 1.0
O A:HOH366 4.8 37.6 1.0
O A:HOH311 4.8 34.1 1.0
OG1 A:THR142 4.9 21.1 1.0
CG A:PRO143 4.9 20.9 1.0
N A:THR142 4.9 19.8 1.0
ND2 A:ASN144 5.0 30.6 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 03:33:30 2025

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