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

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

All present enzymatic activity of Aspartyl/Asparaginyl Beta-Hydroxylase (Asph) Oxygenase and Tpr Domains in Complex with Manganese and 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 2-Oxoglutarate, PDB code: 6yyu 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) 85.44 / 2.11
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.791, 70.003, 170.87, 90, 90, 90
R / Rfree (%) 20.2 / 23.1

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 2-Oxoglutarate (pdb code 6yyu). 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 2-Oxoglutarate, PDB code: 6yyu:

Manganese binding site 1 out of 1 in 6yyu

Go back to Manganese Binding Sites List in 6yyu
Manganese binding site 1 out of 1 in the Aspartyl/Asparaginyl Beta-Hydroxylase (Asph) Oxygenase and Tpr Domains in Complex with Manganese and 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 2-Oxoglutarate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn801

b:35.2
occ:1.00
 O1 A:AKG802 1.6 72.0 1.0
NE2 A:HIS725 2.1 36.9 1.0
O A:HOH905 2.1 34.2 1.0
NE2 A:HIS679 2.3 44.2 1.0
C1 A:AKG802 2.3 66.7 1.0
O A:HOH937 2.4 48.9 1.0
O5 A:AKG802 2.5 70.2 1.0
C2 A:AKG802 2.8 57.6 1.0
CE1 A:HIS679 3.0 42.1 1.0
HE1 A:HIS679 3.0 61.0 1.0
CD2 A:HIS725 3.1 37.7 1.0
CE1 A:HIS725 3.1 31.7 1.0
HD2 A:HIS725 3.2 58.3 1.0
HE1 A:HIS725 3.3 45.9 1.0
CD2 A:HIS679 3.4 31.6 1.0
O2 A:AKG802 3.5 28.4 1.0
HH11 A:ARG688 3.5 44.6 1.0
HD2 A:HIS679 3.7 37.9 1.0
HH12 A:ARG688 3.8 44.6 1.0
NH1 A:ARG688 4.0 30.5 1.0
ND1 A:HIS679 4.2 34.6 1.0
ND1 A:HIS725 4.2 37.8 1.0
HB2 A:ASP721 4.2 42.6 1.0
CG A:HIS725 4.2 28.4 1.0
C3 A:AKG802 4.3 52.6 1.0
CG A:HIS679 4.4 32.8 1.0
OD2 A:ASP721 4.6 31.0 1.0
H32 A:AKG802 4.6 63.2 1.0
HD13 A:LEU619 4.6 83.1 1.0
H31 A:AKG802 4.8 63.2 1.0
HZ A:PHE719 4.8 37.2 1.0
HD2 A:ARG688 4.9 66.0 1.0
HD1 A:HIS679 4.9 43.6 1.0
HE2 A:PHE719 5.0 50.8 1.0
H42 A:AKG802 5.0 64.5 1.0
HH2 A:TRP625 5.0 80.5 1.0
HD1 A:HIS725 5.0 58.0 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 07:56:10 2024

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