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Chlorine in PDB 4i69: Crystal Structure of the K463A Mutant of the Rrm Domain of Rna Helicase Hera From T. Thermophilus

Enzymatic activity of Crystal Structure of the K463A Mutant of the Rrm Domain of Rna Helicase Hera From T. Thermophilus

All present enzymatic activity of Crystal Structure of the K463A Mutant of the Rrm Domain of Rna Helicase Hera From T. Thermophilus:
3.6.4.13;

Protein crystallography data

The structure of Crystal Structure of the K463A Mutant of the Rrm Domain of Rna Helicase Hera From T. Thermophilus, PDB code: 4i69 was solved by M.G.Rudolph, D.Klostermeier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.63 / 1.79
Space group P 31
Cell size a, b, c (Å), α, β, γ (°) 49.221, 49.221, 78.830, 90.00, 90.00, 120.00
R / Rfree (%) 19.5 / 24.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the K463A Mutant of the Rrm Domain of Rna Helicase Hera From T. Thermophilus (pdb code 4i69). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of the K463A Mutant of the Rrm Domain of Rna Helicase Hera From T. Thermophilus, PDB code: 4i69:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 4i69

Go back to Chlorine Binding Sites List in 4i69
Chlorine binding site 1 out of 4 in the Crystal Structure of the K463A Mutant of the Rrm Domain of Rna Helicase Hera From T. Thermophilus


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 K463A Mutant of the Rrm Domain of Rna Helicase Hera From T. Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl601

b:39.7
occ:1.00
 NH1 A:ARG480 2.9 33.4 1.0
CD A:ARG480 3.6 52.7 1.0
CZ A:ARG480 4.0 37.7 1.0
NE A:ARG480 4.2 48.3 1.0
CG A:ARG480 4.8 42.0 1.0

Chlorine binding site 2 out of 4 in 4i69

Go back to Chlorine Binding Sites List in 4i69
Chlorine binding site 2 out of 4 in the Crystal Structure of the K463A Mutant of the Rrm Domain of Rna Helicase Hera From T. Thermophilus


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the K463A Mutant of the Rrm Domain of Rna Helicase Hera From T. Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl601

b:28.2
occ:1.00
 NH1 B:ARG449 2.4 36.0 1.0
O B:HOH723 2.8 23.1 1.0
CZ B:ARG449 3.4 30.4 1.0
OG B:SER446 3.8 21.8 1.0
N B:ARG509 3.9 33.0 1.0
NH2 B:ARG449 3.9 33.7 1.0
CA B:ALA508 4.4 26.5 1.0
CG B:ARG449 4.4 20.7 1.0
NE B:ARG449 4.4 29.6 1.0
CB B:ALA508 4.4 23.8 1.0
CB B:ARG509 4.5 29.7 1.0
C B:ALA508 4.6 30.1 1.0
CG B:PRO448 4.6 19.8 1.0
CD B:ARG509 4.7 46.6 1.0
CB B:SER446 4.7 22.6 1.0
CD B:ARG449 4.7 22.7 1.0
CA B:ARG509 4.8 28.6 1.0
CB B:PRO448 4.8 20.4 1.0
CG B:ARG509 4.8 38.0 1.0
CD B:PRO448 5.0 19.9 1.0
O B:ARG509 5.0 30.5 1.0

Chlorine binding site 3 out of 4 in 4i69

Go back to Chlorine Binding Sites List in 4i69
Chlorine binding site 3 out of 4 in the Crystal Structure of the K463A Mutant of the Rrm Domain of Rna Helicase Hera From T. Thermophilus


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of the K463A Mutant of the Rrm Domain of Rna Helicase Hera From T. Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl602

b:32.5
occ:1.00
 NH1 B:ARG493 3.5 29.8 1.0
NE B:ARG493 3.6 27.4 1.0
CZ B:ARG493 3.9 27.5 1.0
CB B:ARG492 4.4 27.6 1.0
CD B:ARG493 4.7 23.8 1.0
CG B:ARG493 4.7 22.8 1.0

Chlorine binding site 4 out of 4 in 4i69

Go back to Chlorine Binding Sites List in 4i69
Chlorine binding site 4 out of 4 in the Crystal Structure of the K463A Mutant of the Rrm Domain of Rna Helicase Hera From T. Thermophilus


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of the K463A Mutant of the Rrm Domain of Rna Helicase Hera From T. Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl601

b:41.6
occ:1.00
 NH1 C:ARG503 3.2 41.1 1.0
NE A:ARG487 3.5 37.4 1.0
CG2 C:THR504 3.8 28.8 1.0
NH2 A:ARG487 3.9 35.0 1.0
CZ A:ARG487 4.0 37.3 1.0
CZ C:ARG503 4.1 37.6 1.0
N C:ARG503 4.2 19.5 1.0
CB C:SER502 4.2 24.7 1.0
CD A:ARG487 4.4 38.6 1.0
CA C:SER502 4.7 22.8 1.0
CG C:ARG503 4.7 25.9 1.0
N C:THR504 4.7 22.8 1.0
NH2 C:ARG503 4.8 46.1 1.0
NE C:ARG503 4.9 33.4 1.0
CB C:ARG503 5.0 20.3 1.0
C C:SER502 5.0 19.8 1.0
CD C:ARG503 5.0 25.7 1.0

Reference:

L.Steimer, J.P.Wurm, M.H.Linden, M.G.Rudolph, J.Wohnert, D.Klostermeier. Recognition of Two Distinct Elements in the Rna Substrate By the Rna-Binding Domain of the T. Thermophilus Dead Box Helicase Hera. Nucleic Acids Res. V. 41 6259 2013.
ISSN: ISSN 0305-1048
PubMed: 23625962
DOI: 10.1093/NAR/GKT323
Page generated: Sat Dec 12 10:44:51 2020

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