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Manganese in PDB 8jdu: Crystal Structure of Mldhd in Complex with 2-Ketovaleric Acid

Enzymatic activity of Crystal Structure of Mldhd in Complex with 2-Ketovaleric Acid

All present enzymatic activity of Crystal Structure of Mldhd in Complex with 2-Ketovaleric Acid:
1.1.2.4;

Protein crystallography data

The structure of Crystal Structure of Mldhd in Complex with 2-Ketovaleric Acid, PDB code: 8jdu was solved by S.Jin, X.Chen, J.Yang, J.Ding, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.57 / 1.67
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 81.727, 102.96, 122.278, 90, 90, 90
R / Rfree (%) 18 / 19.9

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Mldhd in Complex with 2-Ketovaleric Acid (pdb code 8jdu). 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 Crystal Structure of Mldhd in Complex with 2-Ketovaleric Acid, PDB code: 8jdu:

Manganese binding site 1 out of 1 in 8jdu

Go back to Manganese Binding Sites List in 8jdu
Manganese binding site 1 out of 1 in the Crystal Structure of Mldhd in Complex with 2-Ketovaleric Acid


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Mldhd in Complex with 2-Ketovaleric Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn502

b:25.1
occ:0.42
OE1 A:GLU442 2.1 29.4 1.0
O07 A:69O503 2.2 28.2 1.0
NE2 A:HIS405 2.4 29.4 1.0
O05 A:69O503 2.5 29.2 1.0
NE2 A:HIS398 2.5 28.2 1.0
O4 A:FAD501 2.7 27.5 1.0
C06 A:69O503 3.0 28.9 0.7
C04 A:69O503 3.1 29.5 0.5
C4 A:FAD501 3.1 28.0 1.0
CD A:GLU442 3.2 30.7 1.0
CD2 A:HIS398 3.3 27.8 1.0
CE1 A:HIS405 3.3 26.8 1.0
CD2 A:HIS405 3.4 29.8 1.0
CE1 A:HIS398 3.5 26.3 1.0
N3 A:FAD501 3.5 23.3 1.0
OE2 A:GLU442 3.6 28.6 1.0
C4X A:FAD501 3.9 25.4 1.0
NE2 A:HIS443 4.1 25.1 1.0
O08 A:69O503 4.1 33.6 1.0
NH2 A:ARG347 4.3 29.0 1.0
O A:HOH702 4.3 28.8 1.0
N5 A:FAD501 4.3 26.8 1.0
O A:HOH634 4.4 31.2 1.0
CG A:HIS398 4.4 23.9 1.0
ND1 A:HIS405 4.4 28.7 1.0
ND1 A:HIS398 4.5 26.7 1.0
CG A:HIS405 4.5 25.3 1.0
C03 A:69O503 4.5 37.2 1.0
C2 A:FAD501 4.5 23.6 1.0
CG A:GLU442 4.5 23.2 1.0
C10 A:FAD501 4.8 23.6 1.0
CD2 A:HIS443 4.9 27.1 1.0
CE1 A:HIS443 5.0 26.4 1.0

Reference:

S.Jin, X.Chen, J.Yang, J.Ding. Lactate Dehydrogenase D Is A General Dehydrogenase For D-2-Hydroxyacids Containing Hydrophobic Moieties and Plays An Important Role in the Pathogenesis of D-Lactic Acidosis To Be Published.
Page generated: Sun Aug 17 01:23:54 2025

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