Magnesium in PDB 3tpt: Structure of Hipa(D309Q) Bound to Adp

All present enzymatic activity of Structure of Hipa(D309Q) Bound to Adp:
2.7.11.1;

The structure of Structure of Hipa(D309Q) Bound to Adp, PDB code: 3tpt was solved by M.A.Schumacher, T.Link, R.G.Brennan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.20 / 2.25
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	68.600, 84.430, 69.630, 90.00, 91.66, 90.00
R / Rfree (%)	23.2 / 26.7

The binding sites of Magnesium atom in the Structure of Hipa(D309Q) Bound to Adp (pdb code 3tpt). 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 Hipa(D309Q) Bound to Adp, PDB code: 3tpt:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Structure of Hipa(D309Q) Bound to Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Hipa(D309Q) Bound to Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg441 b:60.3 occ:1.00 OD1 A:ASN314 2.6 32.9 1.0 O2A A:ADP500 2.7 47.5 1.0 O3B A:ADP500 3.1 55.3 1.0 OD2 A:ASP332 3.2 55.2 1.0 O3' A:ADP500 3.3 48.1 1.0 CG A:ASN314 3.5 37.6 1.0 O A:HOH442 3.6 36.0 1.0 O A:LYS313 3.9 31.8 1.0 PA A:ADP500 4.0 50.0 1.0 CE1 A:HIS311 4.0 25.1 1.0 C3' A:ADP500 4.0 48.5 1.0 ND2 A:ASN314 4.1 42.1 1.0 O3A A:ADP500 4.1 52.2 1.0 CA A:GLY153 4.2 48.5 1.0 C A:LYS313 4.2 27.4 1.0 CB A:LYS313 4.3 30.5 1.0 CG A:ASP332 4.3 50.0 1.0 C5' A:ADP500 4.4 49.1 1.0 PB A:ADP500 4.5 52.9 1.0 N A:ASN314 4.5 27.5 1.0 NE2 A:HIS311 4.5 32.4 1.0 CA A:ASN314 4.6 31.9 1.0 O5' A:ADP500 4.6 52.6 1.0 C4' A:ADP500 4.6 48.8 1.0 CB A:ASN314 4.7 35.2 1.0 N A:GLY153 4.7 47.4 1.0 CB A:ASP332 4.7 43.4 1.0 CE1 A:TYR331 4.7 34.3 1.0 CA A:LYS313 4.9 27.7 1.0

Magnesium binding site 2 out of 3 in the Structure of Hipa(D309Q) Bound to Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Hipa(D309Q) Bound to Adp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg441 b:60.0 occ:1.00 O2B B:ADP501 2.7 51.9 1.0 OD1 B:ASP332 2.8 48.7 1.0 OD2 B:ASP332 2.8 45.8 1.0 O B:HOH444 3.1 46.8 1.0 CG B:ASP332 3.2 42.9 1.0 PB B:ADP501 3.4 48.4 1.0 OE1 B:GLN155 3.4 63.5 1.0 O3B B:ADP501 3.4 50.7 1.0 CG B:GLN155 3.7 56.3 1.0 CD B:GLN155 3.9 60.3 1.0 CD1 B:ILE334 3.9 45.2 1.0 OE1 B:GLN309 4.0 48.4 1.0 MG B:MG442 4.3 52.3 1.0 NZ B:LYS181 4.5 37.2 1.0 O3A B:ADP501 4.6 44.8 1.0 O1B B:ADP501 4.6 47.6 1.0 CB B:ASP332 4.7 40.6 1.0 CB B:GLN155 4.9 49.0 1.0 CG1 B:ILE334 5.0 41.6 1.0 CD B:GLN309 5.0 43.7 1.0

Magnesium binding site 3 out of 3 in the Structure of Hipa(D309Q) Bound to Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of Hipa(D309Q) Bound to Adp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg442 b:52.3 occ:1.00 OD1 B:ASN314 2.4 27.4 1.0 O3B B:ADP501 2.4 50.7 1.0 O2A B:ADP501 2.4 48.5 1.0 O B:HOH536 2.5 41.3 1.0 OD2 B:ASP332 2.5 45.8 1.0 O B:HOH444 3.0 46.8 1.0 CG B:ASN314 3.2 31.6 1.0 ND2 B:ASN314 3.3 37.0 1.0 CG B:ASP332 3.4 42.9 1.0 PA B:ADP501 3.6 42.6 1.0 O3A B:ADP501 3.6 44.8 1.0 PB B:ADP501 3.7 48.4 1.0 CE1 B:HIS311 3.7 33.1 1.0 NE2 B:HIS311 3.7 37.5 1.0 CB B:ASP332 3.9 40.6 1.0 O2B B:ADP501 4.0 51.9 1.0 O B:HOH541 4.1 37.9 1.0 OD1 B:ASP332 4.2 48.7 1.0 MG B:MG441 4.3 60.0 1.0 O3' B:ADP501 4.4 42.8 1.0 O1A B:ADP501 4.5 42.6 1.0 CB B:ASN314 4.6 27.6 1.0 O1B B:ADP501 4.7 47.6 1.0 O5' B:ADP501 4.8 44.6 1.0 CA B:GLY153 4.8 37.7 1.0 CA B:ASN314 4.9 29.2 1.0 C5' B:ADP501 4.9 40.4 1.0 ND1 B:HIS311 5.0 30.9 1.0 C3' B:ADP501 5.0 37.6 1.0 O B:LYS313 5.0 28.8 1.0

M.A.Schumacher, J.Min, T.M.Link, Z.Guan, W.Xu, Y.H.Ahn, E.J.Soderblom, J.M.Kurie, A.Evdokimov, M.A.Moseley, K.Lewis, R.G.Brennan. Role of Unusual P Loop Ejection and Autophosphorylation in Hipa-Mediated Persistence and Multidrug Tolerance. Cell Rep V. 2 518 2012.
ISSN: ESSN 2211-1247
PubMed: 22999936
DOI: 10.1016/J.CELREP.2012.08.013