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Chlorine in PDB 5g2c: The Crystal Structure of Light-Driven Chloride Pump Clr (T102D) Mutant at pH 4.5.

Protein crystallography data

The structure of The Crystal Structure of Light-Driven Chloride Pump Clr (T102D) Mutant at pH 4.5., PDB code: 5g2c was solved by K.L.Kim, S.K.Kwon, S.H.Jun, J.S.Cha, H.Y.Kim, J.H.Kim, H.S.Cho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 58.28 / 2.31
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 103.441, 50.033, 77.786, 90.00, 131.47, 90.00
R / Rfree (%) 19.5 / 23.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Crystal Structure of Light-Driven Chloride Pump Clr (T102D) Mutant at pH 4.5. (pdb code 5g2c). 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 The Crystal Structure of Light-Driven Chloride Pump Clr (T102D) Mutant at pH 4.5., PDB code: 5g2c:

Chlorine binding site 1 out of 1 in 5g2c

Go back to Chlorine Binding Sites List in 5g2c
Chlorine binding site 1 out of 1 in the The Crystal Structure of Light-Driven Chloride Pump Clr (T102D) Mutant at pH 4.5.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Crystal Structure of Light-Driven Chloride Pump Clr (T102D) Mutant at pH 4.5. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1272

b:58.4
occ:1.00
N A:LYS46 3.1 28.9 1.0
CB A:LYS46 3.3 34.8 1.0
CG A:PRO45 3.7 28.0 1.0
CD A:PRO45 3.7 28.9 1.0
N A:PRO45 3.8 28.3 1.0
CA A:LYS46 3.8 30.9 1.0
CB A:ALA44 3.9 26.3 1.0
C A:PRO45 4.0 28.8 1.0
CA A:PRO45 4.2 28.9 1.0
CB A:PRO45 4.2 29.1 1.0
C A:ALA44 4.3 27.9 1.0
CE A:LYS46 4.5 48.2 1.0
CG A:LYS46 4.6 40.8 1.0
CA A:ALA44 4.7 25.9 1.0
O A:ALA44 4.9 27.5 1.0

Reference:

K.Kim, S.Kwon, S.Jun, J.S.Cha, H.Kim, W.Lee, J.F.Kim, H.Cho. Crystal Structure and Functional Characterization of A Light-Driven Chloride Pump Having An Ntq Motif. Nat.Commun. V. 7 12677 2016.
ISSN: ESSN 2041-1723
PubMed: 27554809
DOI: 10.1038/NCOMMS12677
Page generated: Sat Dec 12 11:46:18 2020

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