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Manganese in PDB 5z2r: Thdp-MN2+ Complex of R395K Variant of Ecmend Soaked with 2- Ketoglutarate For 5 Min

Enzymatic activity of Thdp-MN2+ Complex of R395K Variant of Ecmend Soaked with 2- Ketoglutarate For 5 Min

All present enzymatic activity of Thdp-MN2+ Complex of R395K Variant of Ecmend Soaked with 2- Ketoglutarate For 5 Min:
2.2.1.9;

Protein crystallography data

The structure of Thdp-MN2+ Complex of R395K Variant of Ecmend Soaked with 2- Ketoglutarate For 5 Min, PDB code: 5z2r was solved by M.M.Qin, Z.H.Guo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.63 / 2.30
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 90.630, 90.750, 172.370, 82.91, 75.71, 64.20
R / Rfree (%) 17 / 20.1

Other elements in 5z2r:

The structure of Thdp-MN2+ Complex of R395K Variant of Ecmend Soaked with 2- Ketoglutarate For 5 Min also contains other interesting chemical elements:

Magnesium (Mg) 7 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Thdp-MN2+ Complex of R395K Variant of Ecmend Soaked with 2- Ketoglutarate For 5 Min (pdb code 5z2r). 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 Thdp-MN2+ Complex of R395K Variant of Ecmend Soaked with 2- Ketoglutarate For 5 Min, PDB code: 5z2r:

Manganese binding site 1 out of 1 in 5z2r

Go back to Manganese Binding Sites List in 5z2r
Manganese binding site 1 out of 1 in the Thdp-MN2+ Complex of R395K Variant of Ecmend Soaked with 2- Ketoglutarate For 5 Min


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Thdp-MN2+ Complex of R395K Variant of Ecmend Soaked with 2- Ketoglutarate For 5 Min within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mn602

b:30.0
occ:1.00
O G:GLY471 2.0 18.6 1.0
OD1 G:ASP442 2.0 20.0 1.0
OD1 G:ASN469 2.0 20.5 1.0
O3B G:TD6601 2.0 15.1 1.0
O2A G:TD6601 2.1 21.5 1.0
O G:HOH805 2.3 19.1 1.0
CG G:ASN469 3.0 20.7 1.0
CG G:ASP442 3.1 17.3 1.0
C G:GLY471 3.1 16.9 1.0
PA G:TD6601 3.3 22.4 1.0
PB G:TD6601 3.3 17.6 1.0
ND2 G:ASN469 3.5 20.6 1.0
O3A G:TD6601 3.5 18.2 1.0
OD2 G:ASP442 3.6 16.5 1.0
N G:ASP442 3.8 17.6 1.0
N G:GLY471 3.9 17.4 1.0
N G:GLY472 4.1 16.3 1.0
CA G:GLY471 4.1 16.8 1.0
N G:GLN473 4.1 18.0 1.0
O7 G:TD6601 4.2 24.4 1.0
CA G:GLY472 4.2 16.4 1.0
N G:ASN469 4.2 18.9 1.0
O2B G:TD6601 4.2 14.7 1.0
CB G:ASP442 4.3 16.3 1.0
O G:VAL467 4.3 17.3 1.0
O G:HOH829 4.4 16.7 1.0
O1B G:TD6601 4.4 15.1 1.0
CB G:ASN469 4.4 19.1 1.0
O1A G:TD6601 4.4 18.4 1.0
N G:LEU443 4.5 19.0 1.0
CA G:ASP442 4.6 17.4 1.0
C G:ASN469 4.6 20.7 1.0
CA G:ASN469 4.6 19.2 1.0
CA G:GLY441 4.6 15.1 1.0
N G:ASN470 4.6 20.6 1.0
C G:GLY441 4.7 17.5 1.0
CG G:GLN473 4.7 17.1 1.0
C G:GLY472 4.7 17.9 1.0
C G:ASN470 4.9 19.8 1.0
CG G:LEU443 4.9 20.8 1.0
CB G:GLN473 4.9 18.2 1.0

Reference:

M.M.Qin, H.G.Song, X.Dai, Y.Z.Chen, Z.H.Guo. Two Active Site Arginines Are Critical Determinants of Substrate Binding and Catalysis in Mend: A Thiamine-Dependent Enzyme in Menaquinone Biosynthesis. Biochem. J. V. 475 3651 2018.
ISSN: ESSN 1470-8728
PubMed: 30341164
DOI: 10.1042/BCJ20180548
Page generated: Sun Oct 6 03:37:31 2024

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