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Chlorine in PDB 4ccg: Structure of An E2-E3 Complex

Protein crystallography data

The structure of Structure of An E2-E3 Complex, PDB code: 4ccg was solved by C.Hodson, A.Purkiss, H.Walden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.817 / 2.40
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 109.224, 109.224, 117.728, 90.00, 90.00, 90.00
R / Rfree (%) 21.24 / 24.76

Other elements in 4ccg:

The structure of Structure of An E2-E3 Complex also contains other interesting chemical elements:

Zinc (Zn) 4 atoms
Sodium (Na) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of An E2-E3 Complex (pdb code 4ccg). 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 Structure of An E2-E3 Complex, PDB code: 4ccg:

Chlorine binding site 1 out of 1 in 4ccg

Go back to Chlorine Binding Sites List in 4ccg
Chlorine binding site 1 out of 1 in the Structure of An E2-E3 Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of An E2-E3 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1153

b:72.8
occ:1.00
NE B:ARG9 3.1 54.6 1.0
NH2 B:ARG9 3.4 57.6 1.0
CE2 Y:TYR311 3.7 52.7 1.0
CZ B:ARG9 3.7 61.0 1.0
CG B:MET13 3.9 52.9 1.0
NE2 X:GLN350 3.9 64.9 1.0
CD2 Y:TYR311 4.0 55.7 1.0
CG B:ARG9 4.1 52.7 1.0
CD B:ARG9 4.2 53.3 1.0
CA B:GLU10 4.2 56.0 1.0
CG B:GLU10 4.2 65.0 1.0
CB B:MET13 4.3 47.0 1.0
O B:ARG9 4.3 61.1 1.0
N B:GLU10 4.4 55.9 1.0
C B:ARG9 4.4 57.4 1.0
CZ Y:TYR311 4.4 52.6 1.0
ND2 B:ASN103 4.5 61.3 1.0
CD X:GLN350 4.6 62.6 1.0
CB B:ARG9 4.6 53.7 1.0
OE1 X:GLN350 4.6 57.8 1.0
CB B:GLU10 4.8 61.0 1.0
OH Y:TYR311 4.8 50.8 1.0
CG Y:TYR311 4.9 55.0 1.0

Reference:

C.Hodson, A.Purkiss, J.A.Miles, H.Walden. Structure of the Human Fancl Ring-UBE2T Complex Reveals Determinants of Cognate E3-E2 Selection. Structure V. 22 337 2014.
ISSN: ISSN 0969-2126
PubMed: 24389026
DOI: 10.1016/J.STR.2013.12.004
Page generated: Sat Dec 12 10:29:05 2020

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