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Manganese in PDB 8re6: Aspartyl/Asparaginyl Beta-Hydroxylase (Asph) R735Q Variant in Complex with Mn, 2-Oxoglutarate and A Factor X Derived Peptide Fragment

Enzymatic activity of Aspartyl/Asparaginyl Beta-Hydroxylase (Asph) R735Q Variant in Complex with Mn, 2-Oxoglutarate and A Factor X Derived Peptide Fragment

All present enzymatic activity of Aspartyl/Asparaginyl Beta-Hydroxylase (Asph) R735Q Variant in Complex with Mn, 2-Oxoglutarate and A Factor X Derived Peptide Fragment:
1.14.11.16;

Protein crystallography data

The structure of Aspartyl/Asparaginyl Beta-Hydroxylase (Asph) R735Q Variant in Complex with Mn, 2-Oxoglutarate and A Factor X Derived Peptide Fragment, PDB code: 8re6 was solved by A.Brasnett, C.Hou, P.Rabe, L.Brewitz, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 51.03 / 1.92
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.103, 90.858, 123.352, 90, 90, 90
R / Rfree (%) 19.4 / 21.6

Manganese Binding Sites:

The binding sites of Manganese atom in the Aspartyl/Asparaginyl Beta-Hydroxylase (Asph) R735Q Variant in Complex with Mn, 2-Oxoglutarate and A Factor X Derived Peptide Fragment (pdb code 8re6). 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) R735Q Variant in Complex with Mn, 2-Oxoglutarate and A Factor X Derived Peptide Fragment, PDB code: 8re6:

Manganese binding site 1 out of 1 in 8re6

Go back to Manganese Binding Sites List in 8re6
Manganese binding site 1 out of 1 in the Aspartyl/Asparaginyl Beta-Hydroxylase (Asph) R735Q Variant in Complex with Mn, 2-Oxoglutarate and A Factor X Derived Peptide Fragment


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) R735Q Variant in Complex with Mn, 2-Oxoglutarate and A Factor X Derived Peptide Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn801

b:30.2
occ:1.00
 O A:HOH997 2.0 31.2 1.0
O2 A:AKG802 2.1 33.8 1.0
NE2 A:HIS725 2.1 29.9 1.0
O A:HOH970 2.1 33.7 1.0
O5 A:AKG802 2.2 31.5 1.0
NE2 A:HIS679 2.3 30.2 1.0
C2 A:AKG802 2.9 39.3 1.0
C1 A:AKG802 2.9 31.6 1.0
CD2 A:HIS725 3.0 27.5 1.0
CE1 A:HIS679 3.0 33.8 1.0
CE1 A:HIS725 3.2 31.6 1.0
CD2 A:HIS679 3.4 32.2 1.0
NH1 A:ARG688 4.1 31.4 1.0
O1 A:AKG802 4.1 35.1 1.0
O4 A:AKG802 4.2 37.5 1.0
ND1 A:HIS679 4.2 34.3 1.0
CG A:HIS725 4.2 29.4 1.0
ND1 A:HIS725 4.2 30.4 1.0
O B:ASP103 4.3 34.1 1.0
CG A:HIS679 4.4 36.0 1.0
C3 A:AKG802 4.4 35.6 1.0
OD2 A:ASP721 4.4 33.0 1.0
CB B:ASP103 4.7 33.6 1.0
CB A:ASP721 4.8 28.1 1.0
OD1 B:ASP103 4.9 36.9 1.0
CG B:ASP103 5.0 32.0 1.0

Reference:

A.Brasnett, C.Hou, P.Rabe, L.Brewitz, C.J.Schofield. Aspartyl/Asparaginyl Beta-Hydroxylase (Asph) R735Q Variant in Complex with Mn, 2-Oxoglutarate and A Factor X Derived Peptide Fragment To Be Published.
Page generated: Sat Feb 8 22:55:09 2025

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