Arsenic in PDB 6h2p: Crystal Structure of ARG184GLN Mutant of Human Prolidase with Mn Ions and Cacodylate Ligand

All present enzymatic activity of Crystal Structure of ARG184GLN Mutant of Human Prolidase with Mn Ions and Cacodylate Ligand:
3.4.13.9;

The structure of Crystal Structure of ARG184GLN Mutant of Human Prolidase with Mn Ions and Cacodylate Ligand, PDB code: 6h2p was solved by P.Wilk, R.Piwowarczyk, M.S.Weiss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.99 / 1.48
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	103.453, 107.075, 216.543, 90.00, 90.00, 90.00
R / Rfree (%)	14.8 / 17

The structure of Crystal Structure of ARG184GLN Mutant of Human Prolidase with Mn Ions and Cacodylate Ligand also contains other interesting chemical elements:

Manganese

(Mn)

4 atoms

The binding sites of Arsenic atom in the Crystal Structure of ARG184GLN Mutant of Human Prolidase with Mn Ions and Cacodylate Ligand (pdb code 6h2p). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the Crystal Structure of ARG184GLN Mutant of Human Prolidase with Mn Ions and Cacodylate Ligand, PDB code: 6h2p:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in the Crystal Structure of ARG184GLN Mutant of Human Prolidase with Mn Ions and Cacodylate Ligand


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of ARG184GLN Mutant of Human Prolidase with Mn Ions and Cacodylate Ligand within 5.0Å range: probe atom residue distance (Å) B Occ A:As503 b:25.9 occ:1.00 AS A:CAC503 0.0 25.9 1.0 O2 A:CAC503 1.7 25.3 1.0 O1 A:CAC503 1.7 19.3 1.0 C2 A:CAC503 2.0 54.7 1.0 C1 A:CAC503 2.0 50.9 1.0 HE2 A:HIS377 3.0 23.9 1.0 O A:HOH644 3.3 35.8 1.0 MN A:MN502 3.3 13.8 0.9 MN A:MN501 3.3 14.2 0.9 HE1 A:HIS255 3.4 34.7 0.4 NE2 A:HIS377 3.8 19.9 1.0 OD2 A:ASP276 3.9 14.9 1.0 OD2 A:ASP287 4.1 16.0 1.0 CE1 A:HIS255 4.1 28.9 0.4 OD1 A:ASP287 4.3 16.7 1.0 OE1 A:GLU412 4.4 24.6 1.0 NE2 A:HIS370 4.5 12.6 1.0 HE1 A:HIS377 4.5 21.6 1.0 CE1 A:HIS377 4.5 18.0 1.0 HG21 A:VAL376 4.5 27.1 1.0 CG A:ASP287 4.6 15.0 1.0 HD12 A:ILE244 4.6 27.9 1.0 HD11 A:ILE244 4.7 27.9 1.0 HG22 A:VAL376 4.7 27.1 1.0 OE2 A:GLU412 4.7 16.1 1.0 CG A:ASP276 4.7 14.9 1.0 CD2 A:HIS377 4.7 18.2 1.0 ND1 A:HIS255 4.8 24.1 0.4 HD2 A:HIS377 4.8 21.9 1.0 OE2 A:GLU452 4.9 15.5 1.0 OD1 A:ASP276 4.9 15.7 1.0 NE2 A:HIS255 5.0 36.5 0.4

Arsenic binding site 2 out of 2 in the Crystal Structure of ARG184GLN Mutant of Human Prolidase with Mn Ions and Cacodylate Ligand


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Crystal Structure of ARG184GLN Mutant of Human Prolidase with Mn Ions and Cacodylate Ligand within 5.0Å range: probe atom residue distance (Å) B Occ B:As503 b:27.8 occ:0.88 AS B:CAC503 0.0 27.8 0.9 O2 B:CAC503 1.7 20.2 0.9 O1 B:CAC503 1.8 53.5 0.9 C1 B:CAC503 2.0 40.8 0.9 C2 B:CAC503 2.0 28.1 0.9 HE2 B:HIS377 3.0 22.0 1.0 MN B:MN501 3.3 15.7 1.0 MN B:MN502 3.3 16.3 1.0 O B:HOH864 3.5 43.8 1.0 NE2 B:HIS377 3.8 18.3 1.0 OD2 B:ASP276 3.9 14.7 1.0 O B:HOH695 3.9 38.1 1.0 OD2 B:ASP287 4.0 14.2 1.0 OE1 B:GLU412 4.2 21.9 1.0 OD1 B:ASP287 4.3 14.7 1.0 NE2 B:HIS370 4.4 15.3 1.0 O B:HOH1131 4.5 57.9 1.0 O B:HOH1239 4.5 41.8 1.0 HE1 B:HIS377 4.5 20.4 1.0 CG B:ASP287 4.5 16.8 1.0 NE2 B:HIS255 4.6 39.3 1.0 CE1 B:HIS377 4.6 17.0 1.0 HG21 B:VAL376 4.6 22.2 1.0 OE2 B:GLU412 4.6 16.2 1.0 HD12 B:ILE244 4.7 28.6 1.0 HG22 B:VAL376 4.7 22.2 1.0 HD2 B:HIS255 4.7 31.4 1.0 HD11 B:ILE244 4.7 28.6 1.0 CG B:ASP276 4.7 15.4 1.0 OE2 B:GLU452 4.8 15.4 1.0 CD2 B:HIS377 4.8 17.8 1.0 CD B:GLU412 4.9 18.0 1.0 HD2 B:HIS377 4.9 21.3 1.0 OE1 B:GLU452 4.9 15.8 1.0 OD1 B:ASP276 4.9 15.0 1.0 CD2 B:HIS255 5.0 26.2 1.0

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