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Chlorine in PDB 1d3a: Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form

Enzymatic activity of Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form

All present enzymatic activity of Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form:
1.1.1.37;

Protein crystallography data

The structure of Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form, PDB code: 1d3a 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) 30.00 / 2.94
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 115.780, 131.330, 125.450, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 24.4

Other elements in 1d3a:

The structure of Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form also contains other interesting chemical elements:

Sodium (Na) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form (pdb code 1d3a). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form, PDB code: 1d3a:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1d3a

Go back to Chlorine Binding Sites List in 1d3a
Chlorine binding site 1 out of 2 in the Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl331

b:44.1
occ:1.00
NZ A:LYS205 3.3 35.0 1.0
N A:ASP306 3.3 33.7 1.0
CB A:ASP306 3.5 34.7 1.0
CE A:LYS205 3.8 25.8 1.0
CA A:ASP306 4.0 22.3 1.0
C A:TRP305 4.2 34.0 1.0
CA A:TRP305 4.3 33.0 1.0
O A:ASP306 4.3 30.9 1.0
CB A:TRP305 4.6 28.6 1.0
C A:ASP306 4.6 22.4 1.0
CG A:ASP306 4.8 46.3 1.0

Chlorine binding site 2 out of 2 in 1d3a

Go back to Chlorine Binding Sites List in 1d3a
Chlorine binding site 2 out of 2 in the Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the Wild Type Halophilic Malate Dehydrogenase in the Apo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl331

b:37.5
occ:1.00
NZ B:LYS205 3.4 34.6 1.0
N B:ASP306 3.4 39.9 1.0
CB B:ASP306 3.5 52.3 1.0
CE B:LYS205 3.8 23.7 1.0
CA B:ASP306 4.0 44.8 1.0
C B:TRP305 4.3 33.7 1.0
CA B:TRP305 4.3 32.3 1.0
O B:ASP306 4.3 54.0 1.0
CB B:TRP305 4.5 31.5 1.0
C B:ASP306 4.7 48.4 1.0
CG B:ASP306 4.9 56.3 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: Thu Jul 10 16:37:17 2025

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