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Magnesium in PDB 2cdn: Crystal Structure of Mycobacterium Tuberculosis Adenylate Kinase Complexed with Two Molecules of Adp and Mg

Enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Adenylate Kinase Complexed with Two Molecules of Adp and Mg

All present enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Adenylate Kinase Complexed with Two Molecules of Adp and Mg:
2.7.4.3;

Protein crystallography data

The structure of Crystal Structure of Mycobacterium Tuberculosis Adenylate Kinase Complexed with Two Molecules of Adp and Mg, PDB code: 2cdn was solved by M.Bellinzoni, A.Haouz, M.Grana, H.Munier-Lehmann, P.M.Alzari, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 64.96 / 1.9
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 36.544, 64.910, 39.773, 90.00, 110.12, 90.00
R / Rfree (%) 16.9 / 21.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Mycobacterium Tuberculosis Adenylate Kinase Complexed with Two Molecules of Adp and Mg (pdb code 2cdn). 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 Mycobacterium Tuberculosis Adenylate Kinase Complexed with Two Molecules of Adp and Mg, PDB code: 2cdn:

Magnesium binding site 1 out of 1 in 2cdn

Go back to Magnesium Binding Sites List in 2cdn
Magnesium binding site 1 out of 1 in the Crystal Structure of Mycobacterium Tuberculosis Adenylate Kinase Complexed with Two Molecules of Adp and Mg


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 Mycobacterium Tuberculosis Adenylate Kinase Complexed with Two Molecules of Adp and Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg200

b:40.7
occ:1.00
 O2B A:ADP201 2.1 19.7 0.5
O2B A:ADP202 2.3 15.8 1.0
O A:HOH2126 2.6 26.5 1.0
O A:HOH2062 2.8 25.2 1.0
PB A:ADP202 3.4 15.9 1.0
PB A:ADP201 3.5 22.9 0.5
O2A A:ADP202 3.5 18.8 1.0
O3B A:ADP202 3.7 15.6 1.0
NH1 A:ARG127 3.8 25.5 1.0
NH1 A:ARG129 4.0 22.4 1.0
O3B A:ADP201 4.0 19.4 0.5
CA A:GLY14 4.1 16.4 1.0
O1A A:ADP201 4.1 16.4 1.0
O A:HOH2084 4.1 29.1 1.0
N A:GLY14 4.1 15.8 1.0
O3A A:ADP202 4.2 16.7 1.0
PA A:ADP202 4.3 17.0 1.0
OD2 A:ASP84 4.3 26.1 1.0
O1B A:ADP201 4.4 16.6 0.5
O3A A:ADP201 4.5 17.2 1.0
PA A:ADP201 4.5 17.8 1.0
OD1 A:ASP84 4.6 24.2 1.0
O2A A:ADP201 4.7 18.7 1.0
O1A A:ADP202 4.7 18.5 1.0
O1B A:ADP202 4.7 15.4 1.0
CG A:ASP84 4.9 21.1 1.0
O A:HOH2054 4.9 41.3 1.0
CZ A:ARG127 5.0 25.1 1.0

Reference:

M.Bellinzoni, A.Haouz, M.Grana, H.Munier-Lehmann, W.Shepard, P.M.Alzari. The Crystal Structure of Mycobacterium Tuberculosis Adenylate Kinase in Complex with Two Molecules of Adp and MG2+ Supports An Associative Mechanism For Phosphoryl Transfer. Protein Sci. V. 15 1489 2006.
ISSN: ISSN 0961-8368
PubMed: 16672241
DOI: 10.1110/PS.062163406
Page generated: Tue Aug 13 22:14:48 2024

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