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Magnesium in PDB 6pxj: Crystal Structure of Human Thrombin Mutant I16T

Enzymatic activity of Crystal Structure of Human Thrombin Mutant I16T

All present enzymatic activity of Crystal Structure of Human Thrombin Mutant I16T:
3.4.21.5;

Protein crystallography data

The structure of Crystal Structure of Human Thrombin Mutant I16T, PDB code: 6pxj was solved by B.Stojanovski, Z.Chen, S.K.Koester, L.A.Pelc, E.Di Cera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.77 / 1.70
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 81.595, 151.399, 50.561, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 20.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human Thrombin Mutant I16T (pdb code 6pxj). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Human Thrombin Mutant I16T, PDB code: 6pxj:

Magnesium binding site 1 out of 1 in 6pxj

Go back to Magnesium Binding Sites List in 6pxj
Magnesium binding site 1 out of 1 in the Crystal Structure of Human Thrombin Mutant I16T


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Human Thrombin Mutant I16T within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg301

b:37.7
occ:1.00
O B:HOH477 2.0 43.1 1.0
OD2 B:ASP189 2.0 41.5 1.0
O B:HOH563 2.1 38.5 1.0
O B:HOH603 2.1 36.6 1.0
O B:HOH461 2.1 42.7 1.0
O B:HOH545 2.2 33.8 1.0
CG B:ASP189 3.1 38.6 1.0
OD1 B:ASP189 3.5 36.7 1.0
O B:HOH433 3.9 36.6 1.0
N B:CYS220 4.2 35.7 1.0
O B:HOH441 4.3 37.8 1.0
O B:ARG187 4.3 36.9 1.0
CB B:ASP189 4.4 29.7 1.0
O B:HOH498 4.5 44.9 1.0
O B:HOH462 4.6 27.8 1.0
CA B:CYS220 4.6 38.0 1.0
O B:CYS220 4.9 44.8 1.0
CG2 B:VAL17 4.9 41.4 1.0

Reference:

B.M.Stojanovski, Z.Chen, S.K.Koester, L.A.Pelc, E.Di Cera. Role of the I16-D194 Ionic Interaction in the Trypsin Fold. Sci Rep V. 9 18035 2019.
ISSN: ESSN 2045-2322
PubMed: 31792294
DOI: 10.1038/S41598-019-54564-6
Page generated: Tue Oct 1 15:20:54 2024

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