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Chlorine in PDB 6csn: Crystal Structure of the Designed Light-Gated Anion Channel Ic++ at PH8.5

Protein crystallography data

The structure of Crystal Structure of the Designed Light-Gated Anion Channel Ic++ at PH8.5, PDB code: 6csn was solved by H.E.Kato, Y.Kim, K.Yamashita, B.K.Kobilka, K.Deisseroth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.55 / 2.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 60.520, 142.520, 91.250, 90.00, 90.00, 90.00
R / Rfree (%) 23.2 / 26

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Designed Light-Gated Anion Channel Ic++ at PH8.5 (pdb code 6csn). 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 the Designed Light-Gated Anion Channel Ic++ at PH8.5, PDB code: 6csn:

Chlorine binding site 1 out of 1 in 6csn

Go back to Chlorine Binding Sites List in 6csn
Chlorine binding site 1 out of 1 in the Crystal Structure of the Designed Light-Gated Anion Channel Ic++ at PH8.5


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 the Designed Light-Gated Anion Channel Ic++ at PH8.5 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl403

b:81.6
occ:1.00
NE A:ARG281 2.8 59.4 1.0
NH1 A:ARG281 3.2 59.2 1.0
CZ A:ARG281 3.5 61.4 1.0
NE A:ARG156 3.5 58.2 1.0
CE1 A:PHE141 3.7 62.3 1.0
CD A:ARG281 3.9 57.3 1.0
CG2 A:VAL146 4.1 39.1 1.0
CB A:ARG156 4.1 51.6 1.0
CD A:ARG156 4.1 55.7 1.0
CB A:ARG281 4.2 51.2 1.0
OD1 A:ASN285 4.3 64.8 1.0
CD1 A:PHE141 4.3 56.6 1.0
CZ A:PHE141 4.4 64.3 1.0
CZ A:ARG156 4.5 62.2 1.0
NH2 A:ARG156 4.5 66.5 1.0
ND2 A:ASN285 4.5 72.3 1.0
CG A:ARG156 4.6 56.6 1.0
CG A:ARG281 4.6 55.9 1.0
CG1 A:VAL146 4.7 43.3 1.0
NH2 A:ARG281 4.8 64.0 1.0
CA A:ARG156 4.8 47.5 1.0
CG A:ASN285 4.9 68.2 1.0
O A:ARG281 4.9 65.6 1.0
N A:ARG156 5.0 46.0 1.0

Reference:

H.E.Kato, Y.S.Kim, J.M.Paggi, K.E.Evans, W.E.Allen, C.Richardson, K.Inoue, S.Ito, C.Ramakrishnan, L.E.Fenno, K.Yamashita, D.Hilger, S.Y.Lee, A.Berndt, K.Shen, H.Kandori, R.O.Dror, B.K.Kobilka, K.Deisseroth. Structural Mechanisms of Selectivity and Gating in Anion Channelrhodopsins. Nature V. 561 349 2018.
ISSN: ESSN 1476-4687
PubMed: 30158697
DOI: 10.1038/S41586-018-0504-5
Page generated: Sat Jul 12 12:32:23 2025

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