Chlorine in PDB 6ljc: Crystal Structure of Fragmin F2-F3 Domains (Calcium and Magnesium Condition)

The structure of Crystal Structure of Fragmin F2-F3 Domains (Calcium and Magnesium Condition), PDB code: 6ljc was solved by S.Takeda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.09 / 1.85
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	115.590, 115.590, 42.220, 90.00, 90.00, 120.00
R / Rfree (%)	18.3 / 20.3

The structure of Crystal Structure of Fragmin F2-F3 Domains (Calcium and Magnesium Condition) also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Calcium	(Ca)	2 atoms

The binding sites of Chlorine atom in the Crystal Structure of Fragmin F2-F3 Domains (Calcium and Magnesium Condition) (pdb code 6ljc). 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 Crystal Structure of Fragmin F2-F3 Domains (Calcium and Magnesium Condition), PDB code: 6ljc:

Chlorine binding site 1 out of 1 in the Crystal Structure of Fragmin F2-F3 Domains (Calcium and Magnesium Condition)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Fragmin F2-F3 Domains (Calcium and Magnesium Condition) within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl405 b:64.4 occ:1.00 OG C:SER266 3.4 34.4 1.0 O C:HOH680 3.5 38.9 1.0 N C:ASP267 3.6 30.5 1.0 O C:HOH583 3.7 49.9 1.0 CG C:LEU268 3.7 46.9 1.0 N C:LEU268 3.7 34.7 1.0 CD1 C:LEU268 3.8 52.6 1.0 CB C:SER266 4.1 31.6 1.0 CA C:SER266 4.2 28.8 1.0 CB C:LEU268 4.2 30.0 1.0 CB C:ASP267 4.3 24.1 1.0 C C:SER266 4.3 24.2 1.0 CA C:ASP267 4.3 29.8 1.0 C C:ASP267 4.6 33.6 1.0 CA C:LEU268 4.6 35.3 1.0 CG C:ASP267 5.0 27.3 1.0 CD2 C:LEU268 5.0 44.5 1.0

S.Takeda, I.Fujiwara, Y.Sugimoto, T.Oda, A.Narita, Y.Maeda. Novel Inter-Domain CA2+-Binding Site in the Gelsolin Superfamily Protein Fragmin. J.Muscle Res.Cell.Motil. 2019.
ISSN: ISSN 0142-4319
PubMed: 31863323
DOI: 10.1007/S10974-019-09571-5