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Manganese in PDB 6vte: Naegleria Gruberi Rna Ligase K170M Mutant with Amp and Mn

Protein crystallography data

The structure of Naegleria Gruberi Rna Ligase K170M Mutant with Amp and Mn, PDB code: 6vte was solved by M.C.Unciuleac, Y.Goldgur, S.Shuman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.70 / 2.10
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 54.916, 54.916, 102.244, 90.00, 90.00, 120.00
R / Rfree (%) 18.9 / 25.3

Manganese Binding Sites:

The binding sites of Manganese atom in the Naegleria Gruberi Rna Ligase K170M Mutant with Amp and Mn (pdb code 6vte). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Naegleria Gruberi Rna Ligase K170M Mutant with Amp and Mn, PDB code: 6vte:

Manganese binding site 1 out of 1 in 6vte

Go back to Manganese Binding Sites List in 6vte
Manganese binding site 1 out of 1 in the Naegleria Gruberi Rna Ligase K170M Mutant with Amp and Mn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Naegleria Gruberi Rna Ligase K170M Mutant with Amp and Mn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn402

b:27.8
occ:1.00
O A:HOH557 2.0 21.1 1.0
O A:HOH580 2.1 34.6 1.0
O A:HOH662 2.1 30.1 1.0
O A:HOH543 2.2 16.9 1.0
O A:HOH571 2.3 24.8 1.0
O3P A:AMP401 2.3 38.3 1.0
P A:AMP401 3.8 57.8 1.0
O4' A:AMP401 4.1 27.6 1.0
OE2 A:GLU227 4.1 33.5 1.0
OE1 A:GLU312 4.1 27.1 1.0
C4' A:AMP401 4.3 30.6 1.0
O A:GLY173 4.3 37.4 1.0
OE2 A:GLU312 4.4 26.2 1.0
OD1 A:ASP172 4.4 23.4 1.0
CE A:MET170 4.4 35.4 1.0
O2P A:AMP401 4.5 57.1 1.0
O1P A:AMP401 4.5 65.1 1.0
C1' A:AMP401 4.5 23.1 1.0
CD A:GLU312 4.7 23.1 1.0
O A:HOH653 4.8 40.7 1.0
O A:LEU171 4.8 23.0 1.0
O5' A:AMP401 4.9 49.5 1.0
O2' A:AMP401 4.9 24.9 1.0

Reference:

M.C.Unciuleac, Y.Goldgur, S.Shuman. Caveat Mutator: Alanine Substitutions For Conserved Amino Acids in Rna Ligase Elicit Unexpected Rearrangements of the Active Site For Lysine Adenylylation Nucleic Acids Res. 2020.
ISSN: ESSN 1362-4962
Page generated: Sun Oct 6 07:37:55 2024

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