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Sodium in PDB 2hlp: Crystal Structure of the E267R Mutant of A Halophilic Malate Dehydrogenase in the Apo Form

Enzymatic activity of Crystal Structure of the E267R Mutant of A Halophilic Malate Dehydrogenase in the Apo Form

All present enzymatic activity of Crystal Structure of the E267R Mutant of A Halophilic Malate Dehydrogenase in the Apo Form:
1.1.1.37;

Protein crystallography data

The structure of Crystal Structure of the E267R Mutant of A Halophilic Malate Dehydrogenase in the Apo Form, PDB code: 2hlp was solved by S.B.Richard, D.Madern, E.Garcin, G.Zaccai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.00 / 2.59
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 114.160, 129.980, 123.450, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 23.6

Other elements in 2hlp:

The structure of Crystal Structure of the E267R Mutant of A Halophilic Malate Dehydrogenase in the Apo Form also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the E267R Mutant of A Halophilic Malate Dehydrogenase in the Apo Form (pdb code 2hlp). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of the E267R Mutant of A Halophilic Malate Dehydrogenase in the Apo Form, PDB code: 2hlp:

Sodium binding site 1 out of 1 in 2hlp

Go back to Sodium Binding Sites List in 2hlp
Sodium binding site 1 out of 1 in the Crystal Structure of the E267R Mutant of A Halophilic Malate Dehydrogenase in the Apo Form


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the E267R Mutant of A Halophilic Malate Dehydrogenase in the Apo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na2001

b:56.7
occ:1.00
 OE2 A:GLU247 2.8 48.0 1.0
OE2 B:GLU247 2.8 37.7 1.0
O B:HOH1025 3.0 35.0 1.0
O B:HOH1050 3.1 47.5 1.0
O A:HOH2058 3.4 57.6 1.0
CD A:GLU247 3.6 36.0 1.0
OE1 A:GLU247 3.6 40.8 1.0
CD B:GLU247 3.7 23.9 1.0
O B:HOH1006 3.7 56.5 1.0
O B:HOH1076 3.8 53.9 1.0
OE1 B:GLU247 3.8 27.0 1.0
O B:HOH1003 3.9 35.3 1.0
OG1 A:THR31 4.9 41.0 1.0

Reference:

S.B.Richard, D.Madern, E.Garcin, G.Zaccai. Halophilic Adaptation: Novel Solvent Protein Interactions Observed in the 2.9 and 2.6 A Resolution Structures of the Wild Type and A Mutant of Malate Dehydrogenase From Haloarcula Marismortui. Biochemistry V. 39 992 2000.
ISSN: ISSN 0006-2960
PubMed: 10653643
DOI: 10.1021/BI991001A
Page generated: Mon Oct 7 02:47:28 2024

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