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Chlorine in PDB 2i1k: Moesin From Spodoptera Frugiperda Reveals the Coiled-Coil Domain at 3.0 Angstrom Resolution

Protein crystallography data

The structure of Moesin From Spodoptera Frugiperda Reveals the Coiled-Coil Domain at 3.0 Angstrom Resolution, PDB code: 2i1k was solved by M.R.Nance, J.J.G.Tesmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 3.00
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 126.940, 126.940, 272.517, 90.00, 90.00, 120.00
R / Rfree (%) 18.1 / 24.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Moesin From Spodoptera Frugiperda Reveals the Coiled-Coil Domain at 3.0 Angstrom Resolution (pdb code 2i1k). 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 Moesin From Spodoptera Frugiperda Reveals the Coiled-Coil Domain at 3.0 Angstrom Resolution, PDB code: 2i1k:

Chlorine binding site 1 out of 1 in 2i1k

Go back to Chlorine Binding Sites List in 2i1k
Chlorine binding site 1 out of 1 in the Moesin From Spodoptera Frugiperda Reveals the Coiled-Coil Domain at 3.0 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Moesin From Spodoptera Frugiperda Reveals the Coiled-Coil Domain at 3.0 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl576

b:25.1
occ:1.00
O A:HOH580 3.1 2.0 1.0
O A:HOH596 3.3 7.9 1.0
N A:GLN463 3.4 14.8 1.0
NE2 A:GLN463 3.6 41.9 1.0
CA A:PRO462 3.7 17.4 1.0
CG A:GLN463 3.8 42.0 1.0
C A:PRO462 4.1 14.8 1.0
CD A:GLN463 4.1 35.7 1.0
CB A:GLN463 4.1 22.6 1.0
CA A:GLN463 4.4 20.1 1.0
CB A:PRO462 4.4 16.4 1.0
O A:THR461 4.7 13.7 1.0
N A:PRO462 4.8 16.1 1.0

Reference:

Q.Li, M.R.Nance, R.Kulikauskas, K.Nyberg, R.Fehon, P.A.Karplus, A.Bretscher, J.J.Tesmer. Self-Masking in An Intact Erm-Merlin Protein: An Active Role For the Central Alpha-Helical Domain. J.Mol.Biol. V. 365 1446 2007.
ISSN: ISSN 0022-2836
PubMed: 17134719
DOI: 10.1016/J.JMB.2006.10.075
Page generated: Thu Jul 10 22:39:52 2025

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