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

Protein crystallography data

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

Resolution Low / High (Å) 38.83 / 2.15
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 115.830, 115.830, 42.110, 90.00, 90.00, 120.00
R / Rfree (%) 19.3 / 21.9

Other elements in 6ljd:

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

Calcium (Ca) 3 atoms

Chlorine Binding Sites:

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

Chlorine binding site 1 out of 1 in 6ljd

Go back to Chlorine Binding Sites List in 6ljd
Chlorine binding site 1 out of 1 in the Crystal Structure of Fragmin F2-F3 Domains (Calcium 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 Condition) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl406

b:71.4
occ:1.00
OG C:SER266 3.1 42.4 1.0
O C:HOH606 3.2 50.5 1.0
N C:ASP267 3.7 44.1 1.0
CD1 C:LEU268 3.7 55.1 1.0
CB C:SER266 3.9 42.5 1.0
N C:LEU268 3.9 49.4 1.0
CA C:SER266 4.1 40.5 1.0
CG C:LEU268 4.2 63.4 1.0
C C:SER266 4.3 41.6 1.0
CB C:LEU268 4.4 49.7 1.0
CB C:ASP267 4.4 35.2 1.0
CA C:ASP267 4.5 45.2 1.0
C C:ASP267 4.7 41.7 1.0
CA C:LEU268 4.8 49.2 1.0

Reference:

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
Page generated: Sun Jul 28 02:53:25 2024

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