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Chlorine in PDB 3hd2: Crystal Structure of E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin

Enzymatic activity of Crystal Structure of E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin

All present enzymatic activity of Crystal Structure of E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin:
2.7.6.3;

Protein crystallography data

The structure of Crystal Structure of E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin, PDB code: 3hd2 was solved by J.Blaszczyk, Y.Li, H.Yan, X.Ji, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.96 / 1.10
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 80.480, 52.870, 36.700, 90.00, 102.71, 90.00
R / Rfree (%) 15.9 / 18.8

Other elements in 3hd2:

The structure of Crystal Structure of E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin (pdb code 3hd2). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin, PDB code: 3hd2:

Chlorine binding site 1 out of 1 in 3hd2

Go back to Chlorine Binding Sites List in 3hd2
Chlorine binding site 1 out of 1 in the Crystal Structure of E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin


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 E. Coli Hppk(Q50A) in Complex with Mgampcpp and Pterin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl192

b:15.7
occ:1.00
O A:HOH264 3.1 17.5 1.0
O A:HOH335 3.7 25.8 1.0
OD1 A:ASN107 3.8 14.9 1.0
CG A:ASN107 4.0 13.3 1.0
ND2 A:ASN107 4.1 12.2 1.0
CB A:ASN107 4.9 12.4 1.0

Reference:

J.Blaszczyk, Y.Li, X.Ji, H.Yan. Role of Loop Coupling in Enzymatic Catalysis and Conformational Dynamics To Be Published.
Page generated: Fri Jul 11 05:55:43 2025

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