Chlorine in PDB 6ytu: Atomic-Resolution Structure of the Coiled-Coil Dimerisation Domain of Human Arc

Protein crystallography data

The structure of Atomic-Resolution Structure of the Coiled-Coil Dimerisation Domain of Human Arc, PDB code: 6ytu was solved by E.I.Hallin, C.Touma, C.R.Bramham, P.Kursula, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100.00 / 0.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 26.844, 42.556, 67.35, 90, 90, 90
R / Rfree (%) 10.3 / 12.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Atomic-Resolution Structure of the Coiled-Coil Dimerisation Domain of Human Arc (pdb code 6ytu). 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 Atomic-Resolution Structure of the Coiled-Coil Dimerisation Domain of Human Arc, PDB code: 6ytu:

Chlorine binding site 1 out of 1 in 6ytu

Go back to Chlorine Binding Sites List in 6ytu
Chlorine binding site 1 out of 1 in the Atomic-Resolution Structure of the Coiled-Coil Dimerisation Domain of Human Arc


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Atomic-Resolution Structure of the Coiled-Coil Dimerisation Domain of Human Arc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl202

b:24.9
occ:0.89
HH22 A:ARG122 2.2 13.3 1.0
HH12 A:ARG122 2.7 13.4 1.0
O A:HOH344 3.0 10.9 1.0
NH2 A:ARG122 3.0 11.1 1.0
NH1 A:ARG122 3.4 11.2 1.0
CZ A:ARG122 3.6 8.9 1.0
HH21 A:ARG122 3.7 13.3 1.0
HH11 A:ARG122 4.1 13.4 1.0
O A:HOH355 4.5 14.6 0.3
O A:HOH332 4.8 36.1 1.0
NE A:ARG122 4.9 9.8 1.0

Reference:

M.S.Eriksen, O.Nikolaienko, E.I.Hallin, S.Grodem, H.J.Bustad, M.I.Flydal, I.Merski, T.Hosokawa, D.Lascu, S.Akerkar, J.Cuellar, J.J.Chambers, R.O'connell, G.Muruganandam, R.Loris, C.Touma, T.Kanhema, Y.Hayashi, M.M.Stratton, J.M.Valpuesta, P.Kursula, A.Martinez, C.R.Bramham. Arc Self-Association and Formation of Virus-Like Capsids Are Mediated By An N-Terminal Helical Coil Motif. Febs J. 2020.
ISSN: ISSN 1742-464X
PubMed: 33175445
DOI: 10.1111/FEBS.15618
Page generated: Sat Apr 3 14:21:09 2021

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