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Manganese in PDB 6yyv: Aspartyl/Asparaginyl Beta-Hydroxylase (Asph) Oxygenase and Tpr Domains in Complex with Manganese and 3-Methyl-2-Oxoglutarate

Enzymatic activity of Aspartyl/Asparaginyl Beta-Hydroxylase (Asph) Oxygenase and Tpr Domains in Complex with Manganese and 3-Methyl-2-Oxoglutarate

All present enzymatic activity of Aspartyl/Asparaginyl Beta-Hydroxylase (Asph) Oxygenase and Tpr Domains in Complex with Manganese and 3-Methyl-2-Oxoglutarate:
1.14.11.16;

Protein crystallography data

The structure of Aspartyl/Asparaginyl Beta-Hydroxylase (Asph) Oxygenase and Tpr Domains in Complex with Manganese and 3-Methyl-2-Oxoglutarate, PDB code: 6yyv was solved by Y.Nakashima, L.Brewitz, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.62 / 1.77
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.802, 70.521, 174.488, 90, 90, 90
R / Rfree (%) 17.3 / 20.8

Manganese Binding Sites:

The binding sites of Manganese atom in the Aspartyl/Asparaginyl Beta-Hydroxylase (Asph) Oxygenase and Tpr Domains in Complex with Manganese and 3-Methyl-2-Oxoglutarate (pdb code 6yyv). 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 Aspartyl/Asparaginyl Beta-Hydroxylase (Asph) Oxygenase and Tpr Domains in Complex with Manganese and 3-Methyl-2-Oxoglutarate, PDB code: 6yyv:

Manganese binding site 1 out of 1 in 6yyv

Go back to Manganese Binding Sites List in 6yyv
Manganese binding site 1 out of 1 in the Aspartyl/Asparaginyl Beta-Hydroxylase (Asph) Oxygenase and Tpr Domains in Complex with Manganese and 3-Methyl-2-Oxoglutarate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Aspartyl/Asparaginyl Beta-Hydroxylase (Asph) Oxygenase and Tpr Domains in Complex with Manganese and 3-Methyl-2-Oxoglutarate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn801

b:24.4
occ:1.00
 O A:HOH997 2.1 27.8 1.0
NE2 A:HIS679 2.2 23.3 1.0
NE2 A:HIS725 2.2 25.0 1.0
O A:HOH1115 2.2 34.5 1.0
O01 A:Q1Z802 2.2 24.0 1.0
O02 A:Q1Z802 2.2 27.4 1.0
C05 A:Q1Z802 2.9 33.8 1.0
C01 A:Q1Z802 3.0 30.7 1.0
CE1 A:HIS725 3.1 28.9 1.0
CD2 A:HIS679 3.1 29.1 1.0
CE1 A:HIS679 3.1 26.8 1.0
CD2 A:HIS725 3.2 27.7 1.0
HE1 A:HIS725 3.2 34.7 1.0
HD2 A:HIS679 3.3 34.9 1.0
HE1 A:HIS679 3.3 32.2 1.0
HD2 A:HIS725 3.4 33.3 1.0
HH11 A:ARG688 3.6 35.2 1.0
HH12 A:ARG688 4.0 35.2 1.0
NH1 A:ARG688 4.1 29.3 1.0
O A:HOH1230 4.1 37.2 1.0
HB2 A:ASP721 4.2 31.0 1.0
O03 A:Q1Z802 4.2 27.1 1.0
ND1 A:HIS679 4.2 21.7 1.0
ND1 A:HIS725 4.2 23.9 1.0
CG A:HIS679 4.3 23.7 1.0
CG A:HIS725 4.3 23.1 1.0
O A:HOH1168 4.3 37.9 1.0
OD2 A:ASP721 4.3 26.2 1.0
C02 A:Q1Z802 4.5 24.8 1.0
HD13 A:LEU619 4.6 39.0 1.0
HZ A:PHE719 4.7 28.2 1.0
HE2 A:PHE719 4.8 30.5 1.0
H06 A:Q1Z802 4.8 29.3 1.0
H01 A:Q1Z802 4.9 29.8 1.0
HD2 A:ARG688 4.9 32.0 1.0
O A:HOH1032 5.0 28.1 1.0

Reference:

L.Brewitz, Y.Nakashima, C.J.Schofield. Synthesis of 2-Oxoglutarate Derivatives and Their Evaluation As Cosubstrates and Inhibitors of Human Aspartate/Asparagine-Beta-Hydroxylase Chem Sci V. 12 1327 2021.
ISSN: ESSN 2041-6539
DOI: 10.1039/D0SC04301J
Page generated: Sun Oct 6 07:56:21 2024

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