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Magnesium in PDB 3hfw: Crystal Structure of Human Adp-Ribosylhydrolase 1 (HARH1)

Enzymatic activity of Crystal Structure of Human Adp-Ribosylhydrolase 1 (HARH1)

All present enzymatic activity of Crystal Structure of Human Adp-Ribosylhydrolase 1 (HARH1):
3.2.2.19;

Protein crystallography data

The structure of Crystal Structure of Human Adp-Ribosylhydrolase 1 (HARH1), PDB code: 3hfw was solved by C.Mueller-Dieckmann, M.S.Weiss, J.Mueller-Dieckmann, F.Koch-Nolte, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.92
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.280, 52.790, 140.340, 90.00, 90.00, 90.00
R / Rfree (%) 15.5 / 18.5

Other elements in 3hfw:

The structure of Crystal Structure of Human Adp-Ribosylhydrolase 1 (HARH1) also contains other interesting chemical elements:

Potassium (K) 1 atom
Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human Adp-Ribosylhydrolase 1 (HARH1) (pdb code 3hfw). 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 Adp-Ribosylhydrolase 1 (HARH1), PDB code: 3hfw:

Magnesium binding site 1 out of 1 in 3hfw

Go back to Magnesium Binding Sites List in 3hfw
Magnesium binding site 1 out of 1 in the Crystal Structure of Human Adp-Ribosylhydrolase 1 (HARH1)


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 Adp-Ribosylhydrolase 1 (HARH1) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg361

b:17.4
occ:1.00
OD2 A:ASP56 1.9 12.0 1.0
OD2 A:ASP304 2.0 12.2 1.0
OD1 A:ASP55 2.1 8.3 1.0
O A:HOH480 2.1 10.8 1.0
O A:HOH481 2.1 13.1 1.0
OG A:SER54 2.2 10.1 1.0
CG A:ASP304 3.1 11.2 1.0
CG A:ASP56 3.2 10.3 1.0
CB A:SER54 3.2 7.7 1.0
CG A:ASP55 3.3 11.1 1.0
OD1 A:ASP304 3.7 11.5 1.0
OD2 A:ASP55 3.9 13.7 1.0
N A:ASP56 3.9 10.0 1.0
O A:HOH384 3.9 15.8 1.0
OD1 A:ASP56 3.9 8.8 1.0
N A:ASP55 4.0 9.3 1.0
OE1 A:GLU25 4.1 8.3 1.0
OG A:SER305 4.1 11.7 1.0
OD1 A:ASP15 4.1 12.9 1.0
O A:HOH386 4.2 9.7 1.0
CB A:ASP56 4.2 11.1 1.0
CB A:ASP304 4.3 10.7 1.0
O A:ARG97 4.3 9.9 1.0
OE2 A:GLU25 4.4 9.6 1.0
CA A:SER54 4.4 8.3 1.0
CB A:ASP55 4.5 10.6 1.0
C A:SER54 4.5 9.3 1.0
CD A:GLU25 4.5 8.2 1.0
CA A:ASP55 4.6 9.9 1.0
O A:ALA98 4.6 9.0 1.0
CA A:ASP56 4.6 10.2 1.0
C A:ASP55 4.7 11.5 1.0

Reference:

F.Koch-Nolte, J.Mueller-Dieckmann, M.S.Weiss, C.Mueller-Dieckmann. Crystal Structure of Human Adp-Ribosylhydrolase 1 To Be Published.
Page generated: Wed Aug 14 15:08:30 2024

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