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Magnesium in PDB 2h28: Crystal Structure of Yeeu From E. Coli. Northeast Structural Genomics Target ER304

Protein crystallography data

The structure of Crystal Structure of Yeeu From E. Coli. Northeast Structural Genomics Target ER304, PDB code: 2h28 was solved by M.Arbing, M.Su, J.Benach, N.K.Karpowich, M.Jiang, R.Xiao, K.Cunningham, L.-C.Ma, C.X.Chen, T.B.Acton, G.T.Montelione, L.Tong, J.F.Hunt, Northeaststructural Genomics Consortium (Nesg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.216, 45.310, 60.185, 90.00, 108.79, 90.00
R / Rfree (%) 22 / 25.3

Other elements in 2h28:

The structure of Crystal Structure of Yeeu From E. Coli. Northeast Structural Genomics Target ER304 also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Yeeu From E. Coli. Northeast Structural Genomics Target ER304 (pdb code 2h28). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Yeeu From E. Coli. Northeast Structural Genomics Target ER304, PDB code: 2h28:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2h28

Go back to Magnesium Binding Sites List in 2h28
Magnesium binding site 1 out of 2 in the Crystal Structure of Yeeu From E. Coli. Northeast Structural Genomics Target ER304


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 Yeeu From E. Coli. Northeast Structural Genomics Target ER304 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg5001

b:50.0
occ:1.00
O A:HIS88 2.7 45.0 1.0
OD1 A:ASP102 2.8 41.7 1.0
O A:HIS86 3.0 65.6 1.0
N A:HIS88 3.2 53.1 1.0
N A:THR103 3.2 35.5 1.0
OG1 A:THR103 3.3 38.6 1.0
C A:HIS88 3.5 47.0 1.0
CG A:ASP102 3.6 42.6 1.0
CA A:HIS88 3.7 49.1 1.0
CD2 A:LEU82 3.7 46.5 1.0
CB A:HIS88 3.7 47.6 1.0
CG2 A:THR103 3.9 35.1 1.0
O A:ASN83 3.9 45.4 1.0
CA A:ASP102 3.9 39.0 1.0
CB A:THR103 4.0 37.5 1.0
C A:ASP102 4.0 37.1 1.0
CA A:THR103 4.1 35.9 1.0
C A:HIS86 4.1 64.9 1.0
C A:GLN87 4.2 56.1 1.0
N A:ASN83 4.2 50.5 1.0
N A:LEU104 4.3 35.4 1.0
OD2 A:ASP102 4.3 44.3 1.0
CB A:ASP102 4.4 39.2 1.0
CA A:GLN87 4.4 58.7 1.0
CA A:LEU82 4.7 50.8 1.0
CG A:HIS88 4.7 48.8 1.0
C A:ASN83 4.7 47.9 1.0
C A:THR103 4.7 34.7 1.0
N A:GLN87 4.7 61.2 1.0
N A:THR89 4.8 43.3 1.0
C A:LEU82 4.9 50.7 1.0
CD2 A:HIS88 5.0 48.9 1.0

Magnesium binding site 2 out of 2 in 2h28

Go back to Magnesium Binding Sites List in 2h28
Magnesium binding site 2 out of 2 in the Crystal Structure of Yeeu From E. Coli. Northeast Structural Genomics Target ER304


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Yeeu From E. Coli. Northeast Structural Genomics Target ER304 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg5002

b:65.8
occ:1.00
O B:GLY21 2.6 33.6 1.0
O A:HOH3014 2.9 38.5 1.0
O A:HOH3049 3.2 52.7 1.0
NH2 A:ARG51 3.3 30.8 1.0
O B:TRP19 3.4 35.9 1.0
CD1 B:TRP19 3.5 34.7 1.0
C B:GLY21 3.8 35.7 1.0
C B:TRP20 3.8 35.7 1.0
CB A:TRP19 3.8 32.2 1.0
N B:GLY21 3.9 35.6 1.0
C B:TRP19 4.0 36.3 1.0
O B:TRP20 4.0 36.0 1.0
CA B:TRP20 4.2 35.3 1.0
NE1 B:TRP19 4.3 34.5 1.0
N A:TRP19 4.3 37.0 1.0
CZ A:ARG51 4.3 30.3 1.0
N B:TRP20 4.4 34.4 1.0
CA B:GLY21 4.4 36.2 1.0
CG B:TRP19 4.4 34.1 1.0
NE A:ARG51 4.5 31.8 1.0
CD2 B:TYR111 4.6 45.4 1.0
CB B:TRP19 4.7 34.5 1.0
CA A:TRP19 4.7 35.2 1.0
CE2 B:TYR111 4.8 47.5 1.0
CG A:TRP19 4.8 31.6 1.0
N B:LEU22 4.9 34.9 1.0

Reference:

M.A.Arbing, S.K.Handelman, A.P.Kuzin, G.Verdon, C.Wang, M.Su, F.P.Rothenbacher, M.Abashidze, M.Liu, J.M.Hurley, R.Xiao, T.Acton, M.Inouye, G.T.Montelione, N.A.Woychik, J.F.Hunt. Crystal Structures of Phd-Doc, Higa, and Yeeu Establish Multiple Evolutionary Links Between Microbial Growth-Regulating Toxin-Antitoxin Systems. Structure V. 18 996 2010.
ISSN: ISSN 0969-2126
PubMed: 20696400
DOI: 10.1016/J.STR.2010.04.018
Page generated: Mon Dec 14 07:25:19 2020

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