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Chlorine in PDB 5mbz: Crystal Structure of SER202PHE Mutant of Human Prolidase with Mn Ions and Glypro Ligand

Enzymatic activity of Crystal Structure of SER202PHE Mutant of Human Prolidase with Mn Ions and Glypro Ligand

All present enzymatic activity of Crystal Structure of SER202PHE Mutant of Human Prolidase with Mn Ions and Glypro Ligand:
3.4.13.9;

Protein crystallography data

The structure of Crystal Structure of SER202PHE Mutant of Human Prolidase with Mn Ions and Glypro Ligand, PDB code: 5mbz was solved by P.Wilk, U.Mueller, H.Dobbek, M.S.Weiss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.79 / 1.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 103.785, 106.945, 216.316, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 17.5

Other elements in 5mbz:

The structure of Crystal Structure of SER202PHE Mutant of Human Prolidase with Mn Ions and Glypro Ligand also contains other interesting chemical elements:

Manganese (Mn) 4 atoms
Sodium (Na) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of SER202PHE Mutant of Human Prolidase with Mn Ions and Glypro Ligand (pdb code 5mbz). 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 SER202PHE Mutant of Human Prolidase with Mn Ions and Glypro Ligand, PDB code: 5mbz:

Chlorine binding site 1 out of 1 in 5mbz

Go back to Chlorine Binding Sites List in 5mbz
Chlorine binding site 1 out of 1 in the Crystal Structure of SER202PHE Mutant of Human Prolidase with Mn Ions and Glypro Ligand


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 SER202PHE Mutant of Human Prolidase with Mn Ions and Glypro Ligand within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl507

b:58.0
occ:1.00
 NE B:ARG444 3.2 47.6 1.0
NE2 B:GLN441 3.3 40.3 0.5
NH2 B:ARG437 3.5 55.6 0.6
NE B:ARG437 3.5 50.2 0.6
NH1 B:ARG444 3.5 44.7 1.0
O B:HOH630 3.6 49.0 1.0
N B:GLN441 3.7 30.9 1.0
CA B:GLN441 3.7 29.1 0.5
CA B:GLN441 3.7 29.3 0.5
CD2 B:LEU440 3.8 36.2 1.0
CZ B:ARG444 3.8 42.4 1.0
O B:ARG437 3.8 51.5 1.0
CG B:LEU440 3.9 33.9 1.0
CZ B:ARG437 3.9 49.5 0.6
CB B:LEU440 4.0 31.9 1.0
CB B:GLN441 4.0 34.7 0.5
CB B:GLN441 4.0 34.9 0.5
C B:LEU440 4.1 32.5 1.0
CG B:ARG444 4.2 37.9 1.0
CA B:ARG437 4.2 37.7 0.6
CA B:ARG437 4.2 39.0 0.4
CD B:ARG444 4.3 36.1 1.0
CD B:GLN441 4.3 50.1 0.5
CB B:ARG437 4.3 43.0 0.6
CB B:ARG437 4.4 42.8 0.4
CG B:ARG437 4.5 49.0 0.4
O B:LEU440 4.5 33.9 1.0
C B:ARG437 4.5 37.6 1.0
CG B:ARG437 4.6 47.6 0.6
CD B:ARG437 4.6 54.2 0.6
CA B:LEU440 4.7 28.1 1.0
CD1 B:LEU426 4.7 41.3 1.0
CG B:GLN441 4.8 37.0 0.5
O B:HOH613 4.8 56.2 1.0

Reference:

P.Wilk, M.Uehlein, R.Piwowarczyk, H.Dobbek, U.Mueller, M.S.Weiss. Structural Basis For Prolidase Deficiency Disease Mechanisms. Febs J. V. 285 3422 2018.
ISSN: ISSN 1742-4658
PubMed: 30066404
DOI: 10.1111/FEBS.14620
Page generated: Sat Jul 12 05:25:25 2025

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