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Manganese in PDB 8jds: Crystal Structure of Mldhd in Complex with Pyruvate

Enzymatic activity of Crystal Structure of Mldhd in Complex with Pyruvate

All present enzymatic activity of Crystal Structure of Mldhd in Complex with Pyruvate:
1.1.2.4;

Protein crystallography data

The structure of Crystal Structure of Mldhd in Complex with Pyruvate, PDB code: 8jds 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) 31.56 / 1.64
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 81.341, 102.74, 122.292, 90, 90, 90
R / Rfree (%) 17.6 / 19.2

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Mldhd in Complex with Pyruvate (pdb code 8jds). 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 Pyruvate, PDB code: 8jds:

Manganese binding site 1 out of 1 in 8jds

Go back to Manganese Binding Sites List in 8jds
Manganese binding site 1 out of 1 in the Crystal Structure of Mldhd in Complex with Pyruvate


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 Pyruvate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn502

b:26.4
occ:0.71
OE2 A:GLU442 2.1 27.0 1.0
O1 A:PYR503 2.2 27.0 1.0
O3 A:PYR503 2.3 28.5 1.0
NE2 A:HIS398 2.3 27.5 1.0
NE2 A:HIS405 2.3 28.3 1.0
O4 A:FAD501 2.6 29.5 1.0
C1 A:PYR503 2.9 31.1 1.0
C2 A:PYR503 2.9 33.1 1.0
C4 A:FAD501 3.0 28.7 1.0
CD A:GLU442 3.2 28.5 1.0
CD2 A:HIS398 3.2 27.1 1.0
CE1 A:HIS405 3.2 27.2 1.0
CD2 A:HIS405 3.3 27.7 1.0
CE1 A:HIS398 3.3 25.1 1.0
N3 A:FAD501 3.5 25.1 1.0
OE1 A:GLU442 3.6 28.7 1.0
C4X A:FAD501 3.9 26.9 1.0
O2 A:PYR503 4.1 36.3 1.0
NE2 A:HIS443 4.1 26.1 1.0
NH2 A:ARG347 4.2 27.8 1.0
N5 A:FAD501 4.2 29.2 1.0
CG A:HIS398 4.3 23.7 1.0
O A:HOH727 4.4 28.1 1.0
ND1 A:HIS405 4.4 28.8 1.0
O A:HOH641 4.4 30.8 1.0
ND1 A:HIS398 4.4 25.0 1.0
C3 A:PYR503 4.4 31.1 1.0
CG A:HIS405 4.4 26.9 1.0
CG A:GLU442 4.4 24.7 1.0
C2 A:FAD501 4.5 24.6 1.0
C10 A:FAD501 4.8 25.1 1.0
CD2 A:HIS443 4.9 24.6 1.0
CE1 A:HIS443 4.9 25.0 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 Oct 6 13:00:03 2024

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