Atomistry » Arsenic » PDB 5yva-6i5j » 6h2p
Atomistry »
  Arsenic »
    PDB 5yva-6i5j »
      6h2p »

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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 6h2p:

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

Arsenic Binding Sites:

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 6h2p

Go back to Arsenic Binding Sites List in 6h2p
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 6h2p

Go back to Arsenic Binding Sites List in 6h2p
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

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 Dec 12 01:49:02 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy