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Magnesium in PDB 4g9o: Crystal Structure of H234A Mutant of Stationary Phase Survival Protein (Sure) From Salmonella Typhimurium

Enzymatic activity of Crystal Structure of H234A Mutant of Stationary Phase Survival Protein (Sure) From Salmonella Typhimurium

All present enzymatic activity of Crystal Structure of H234A Mutant of Stationary Phase Survival Protein (Sure) From Salmonella Typhimurium:
3.1.3.5; 3.1.3.6; 3.6.1.11;

Protein crystallography data

The structure of Crystal Structure of H234A Mutant of Stationary Phase Survival Protein (Sure) From Salmonella Typhimurium, PDB code: 4g9o was solved by Y.K.Mathiharan, M.R.N.Murthy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.00 / 2.12
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 81.040, 98.140, 127.540, 90.00, 90.00, 90.00
R / Rfree (%) 21.9 / 27.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of H234A Mutant of Stationary Phase Survival Protein (Sure) From Salmonella Typhimurium (pdb code 4g9o). 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 H234A Mutant of Stationary Phase Survival Protein (Sure) From Salmonella Typhimurium, PDB code: 4g9o:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4g9o

Go back to Magnesium Binding Sites List in 4g9o
Magnesium binding site 1 out of 2 in the Crystal Structure of H234A Mutant of Stationary Phase Survival Protein (Sure) From Salmonella Typhimurium


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 H234A Mutant of Stationary Phase Survival Protein (Sure) From Salmonella Typhimurium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg305

b:47.1
occ:1.00
OD1 A:ASP9 2.4 37.9 0.9
OG A:SER39 2.5 40.6 1.0
O A:HOH526 2.5 53.9 1.0
OD1 A:ASN92 2.6 30.0 1.0
OD2 A:ASP8 2.7 39.5 1.0
O A:HOH448 2.8 61.6 1.0
CG A:ASP8 3.5 35.8 1.0
CB A:ASP8 3.6 33.8 1.0
CG A:ASN92 3.6 29.7 1.0
CG A:ASP9 3.6 36.6 0.9
O A:HOH405 3.7 38.9 1.0
CB A:SER39 3.7 39.3 1.0
ND2 A:ASN92 3.9 30.8 1.0
OD2 A:ASP9 4.3 38.2 0.9
CA A:SER39 4.3 38.7 1.0
C A:ASP8 4.4 31.1 1.0
N A:ASP9 4.4 31.1 0.9
OD1 A:ASN37 4.4 39.1 1.0
O A:HOH402 4.5 38.9 1.0
N A:SER39 4.6 36.5 1.0
OG1 A:THR106 4.6 27.9 1.0
CA A:ASP8 4.6 31.7 1.0
CA A:ASP9 4.7 32.3 0.9
O A:ASP8 4.7 31.1 1.0
OD1 A:ASP8 4.7 36.1 1.0
CB A:ASP9 4.7 34.2 0.9
CB A:ASN92 5.0 29.0 1.0

Magnesium binding site 2 out of 2 in 4g9o

Go back to Magnesium Binding Sites List in 4g9o
Magnesium binding site 2 out of 2 in the Crystal Structure of H234A Mutant of Stationary Phase Survival Protein (Sure) From Salmonella Typhimurium


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 H234A Mutant of Stationary Phase Survival Protein (Sure) From Salmonella Typhimurium within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg304

b:47.7
occ:1.00
OD1 B:ASP9 2.5 37.6 1.0
OD1 B:ASN92 2.5 33.5 1.0
OD2 B:ASP8 3.4 32.8 0.5
CB B:SER39 3.4 40.3 1.0
CG B:ASP9 3.5 37.2 1.0
CG B:ASN92 3.6 33.1 1.0
CB B:ASP8 3.9 33.8 1.0
ND2 B:ASN92 4.0 33.1 1.0
CG B:ASP8 4.0 33.8 0.5
O B:HOH413 4.0 26.9 1.0
OD2 B:ASP9 4.0 38.8 1.0
CA B:SER39 4.0 38.8 1.0
O B:HOH414 4.1 40.1 1.0
N B:ASP9 4.4 33.5 1.0
O B:HOH449 4.4 50.0 1.0
C B:ASP8 4.5 33.9 1.0
OG B:SER39 4.5 43.7 1.0
O B:ALA93 4.6 34.2 1.0
N B:SER39 4.6 37.2 1.0
CB B:ASP9 4.7 36.0 1.0
CA B:ASP9 4.7 34.5 1.0
CA B:ASP8 4.8 33.9 1.0
OG1 B:THR106 4.8 38.5 1.0
CB B:ASN92 4.9 33.1 1.0
O B:HOH456 4.9 45.4 1.0
N B:ALA93 4.9 32.7 1.0
O B:ASP8 5.0 34.3 1.0

Reference:

Y.K.Mathiharan, A.Pappachan, H.S.Savithri, M.R.N.Murthy. Dramatic Structural Changes Resulting From the Loss of A Crucial Hydrogen Bond in the Hinge Region Involved in C-Terminal Helix Swapping in Sure: A Survival Protein From Salmonella Typhimurium. Plos One V. 8 55978 2013.
ISSN: ESSN 1932-6203
PubMed: 23409101
DOI: 10.1371/JOURNAL.PONE.0055978
Page generated: Mon Dec 14 16:12:10 2020

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