Chlorine in PDB 6dej: The Structure of HCRED7, A Brighter and Red-Shifted Hcred Variant

Protein crystallography data

The structure of The Structure of HCRED7, A Brighter and Red-Shifted Hcred Variant, PDB code: 6dej was solved by T.M.Wannier, S.L.Mayo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.68 / 1.63
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.342, 122.057, 75.254, 90.00, 108.75, 90.00
R / Rfree (%) 17.8 / 21.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Structure of HCRED7, A Brighter and Red-Shifted Hcred Variant (pdb code 6dej). 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 Structure of HCRED7, A Brighter and Red-Shifted Hcred Variant, PDB code: 6dej:

Chlorine binding site 1 out of 1 in 6dej

Go back to Chlorine Binding Sites List in 6dej
Chlorine binding site 1 out of 1 in the The Structure of HCRED7, A Brighter and Red-Shifted Hcred Variant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Structure of HCRED7, A Brighter and Red-Shifted Hcred Variant within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl301

b:67.5
occ:1.00
O D:HOH514 2.2 68.3 1.0
O D:HOH575 2.5 55.2 1.0
O D:HOH577 2.7 49.6 1.0
N D:LYS206 3.1 33.1 1.0
CA D:LYS206 3.8 30.3 1.0
CA D:LYS205 4.0 27.2 1.0
CG D:LYS206 4.0 35.1 1.0
C D:LYS205 4.0 29.9 1.0
NZ D:LYS205 4.3 60.5 1.0
CE D:LYS205 4.4 57.3 1.0
O D:HOH507 4.4 36.0 1.0
CB D:LYS206 4.5 31.7 1.0
CD D:LYS205 4.6 52.0 1.0
O D:LYS204 4.7 36.5 1.0
CB D:LYS205 4.8 34.8 1.0

Reference:

T.M.Wannier, S.K.Gillespie, N.Hutchins, R.S.Mcisaac, S.Y.Wu, Y.Shen, R.E.Campbell, K.S.Brown, S.L.Mayo. Monomerization of Far-Red Fluorescent Proteins. Proc. Natl. Acad. Sci. V. 115 11294 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 30425172
DOI: 10.1073/PNAS.1807449115
Page generated: Sat Dec 12 12:52:57 2020

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