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Magnesium in PDB 1bx4: Structure of Human Adenosine Kinase at 1.50 Angstroms

Enzymatic activity of Structure of Human Adenosine Kinase at 1.50 Angstroms

All present enzymatic activity of Structure of Human Adenosine Kinase at 1.50 Angstroms:
2.7.1.20;

Protein crystallography data

The structure of Structure of Human Adenosine Kinase at 1.50 Angstroms, PDB code: 1bx4 was solved by I.I.Mathews, M.D.Erion, S.E.Ealick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.50
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 65.300, 111.080, 49.690, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 22.6

Other elements in 1bx4:

The structure of Structure of Human Adenosine Kinase at 1.50 Angstroms also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Human Adenosine Kinase at 1.50 Angstroms (pdb code 1bx4). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Structure of Human Adenosine Kinase at 1.50 Angstroms, PDB code: 1bx4:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 1bx4

Go back to Magnesium Binding Sites List in 1bx4
Magnesium binding site 1 out of 3 in the Structure of Human Adenosine Kinase at 1.50 Angstroms


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human Adenosine Kinase at 1.50 Angstroms within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg360

b:11.0
occ:1.00
O A:HOH747 2.2 11.4 1.0
O A:HOH751 2.2 11.2 1.0
O A:HOH746 2.2 10.4 1.0
O A:HOH750 2.2 12.6 1.0
O A:HOH748 2.2 10.8 1.0
O A:HOH749 2.2 9.3 1.0
O A:HOH430 4.0 12.5 1.0
O A:HOH556 4.0 11.8 1.0
O A:SER198 4.1 7.1 1.0
OE2 A:GLU226 4.2 12.0 1.0
O A:HOH515 4.3 17.2 1.0
OD1 A:ASP300 4.4 9.9 1.0
O A:HOH414 4.4 9.3 1.0
OE1 A:GLU226 4.5 11.1 1.0
CL A:CL385 4.6 19.7 1.0
OD1 A:ASN196 4.6 8.4 1.0
O A:ASN296 4.6 10.5 1.0
CA A:GLY299 4.7 6.0 1.0
CD A:GLU226 4.8 12.9 1.0
C A:SER198 4.9 7.9 1.0
ND2 A:ASN223 4.9 11.2 1.0
OE1 A:GLN38 4.9 14.2 1.0
C A:GLY299 5.0 7.2 1.0
CA A:SER198 5.0 6.9 1.0

Magnesium binding site 2 out of 3 in 1bx4

Go back to Magnesium Binding Sites List in 1bx4
Magnesium binding site 2 out of 3 in the Structure of Human Adenosine Kinase at 1.50 Angstroms


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Human Adenosine Kinase at 1.50 Angstroms within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg365

b:15.6
occ:1.00
OD1 A:ASN131 2.1 8.8 1.0
O A:HOH755 2.2 12.9 1.0
OD1 A:ASP130 2.2 11.3 1.0
O A:HOH754 2.2 16.4 1.0
O A:HOH753 2.2 16.3 1.0
O A:HOH752 2.3 16.1 1.0
CG A:ASN131 3.1 9.6 1.0
CG A:ASP130 3.1 12.2 1.0
OD2 A:ASP130 3.5 14.3 1.0
ND2 A:ASN131 3.5 9.6 1.0
OD1 A:ASN36 4.3 16.3 1.0
O A:HOH609 4.3 30.6 1.0
C A:ASP130 4.4 10.5 1.0
CB A:ASN131 4.4 8.3 1.0
N A:ASN131 4.4 9.1 1.0
CB A:ASP130 4.5 10.3 1.0
O A:ASP130 4.6 11.2 1.0
CA A:ASN131 4.6 9.8 1.0
CA A:ASP130 4.8 8.9 1.0

Magnesium binding site 3 out of 3 in 1bx4

Go back to Magnesium Binding Sites List in 1bx4
Magnesium binding site 3 out of 3 in the Structure of Human Adenosine Kinase at 1.50 Angstroms


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of Human Adenosine Kinase at 1.50 Angstroms within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg375

b:28.4
occ:1.00
OG A:SER32 2.2 13.6 1.0
O A:HOH759 2.2 19.7 1.0
O A:HOH758 2.3 23.0 1.0
O A:HOH757 2.3 34.2 1.0
O A:HOH756 2.4 30.3 1.0
O A:HOH402 2.4 25.4 1.0
CB A:SER32 3.1 13.7 1.0
CA A:SER32 3.6 12.1 1.0
O A:ASP29 4.0 15.3 1.0
O A:HOH458 4.2 18.0 1.0
O A:HOH488 4.2 16.6 1.0
N A:SER32 4.3 11.2 1.0
O A:HOH705 4.4 33.4 1.0
C A:SER32 4.9 13.9 1.0

Reference:

I.I.Mathews, M.D.Erion, S.E.Ealick. Structure of Human Adenosine Kinase at 1.5 A Resolution. Biochemistry V. 37 15607 1998.
ISSN: ISSN 0006-2960
PubMed: 9843365
DOI: 10.1021/BI9815445
Page generated: Mon Dec 14 05:48:07 2020

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