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Chlorine 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:

Sodium (Na) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the E267R Mutant of A Halophilic Malate Dehydrogenase in the Apo Form, PDB code: 2hlp:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 2hlp

Go back to Chlorine Binding Sites List in 2hlp
Chlorine binding site 1 out of 2 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 Chlorine with other atoms in the Cl 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:Cl1002

b:44.0
occ:1.00
N A:ASP306 3.3 44.7 1.0
NZ A:LYS205 3.4 24.6 1.0
CB A:ASP306 3.6 48.1 1.0
CE A:LYS205 3.9 33.6 1.0
CA A:ASP306 4.0 44.9 1.0
CA A:TRP305 4.2 45.0 1.0
C A:TRP305 4.2 45.1 1.0
O A:ASP306 4.3 44.8 1.0
C A:ASP306 4.6 44.5 1.0
CB A:TRP305 4.7 42.2 1.0
CG A:ASP306 4.9 62.9 1.0

Chlorine binding site 2 out of 2 in 2hlp

Go back to Chlorine Binding Sites List in 2hlp
Chlorine binding site 2 out of 2 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 Chlorine with other atoms in the Cl binding site number 2 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
B:Cl1001

b:40.3
occ:1.00
N B:ASP306 3.4 43.3 1.0
NZ B:LYS205 3.4 40.9 1.0
CB B:ASP306 3.6 45.5 1.0
CE B:LYS205 4.0 43.1 1.0
CA B:ASP306 4.1 46.4 1.0
C B:TRP305 4.3 39.7 1.0
CA B:TRP305 4.3 36.4 1.0
O B:ASP306 4.4 54.1 1.0
O B:HOH1112 4.6 62.8 1.0
C B:ASP306 4.7 50.3 1.0
CB B:TRP305 4.8 35.3 1.0
CG B:ASP306 5.0 61.9 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: Sat Dec 12 09:07:28 2020

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