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Arsenic in PDB 3rhg: Crystal Structure of Amidohydrolase PMI1525 (Target Efi-500319) From Proteus Mirabilis HI4320

Protein crystallography data

The structure of Crystal Structure of Amidohydrolase PMI1525 (Target Efi-500319) From Proteus Mirabilis HI4320, PDB code: 3rhg was solved by Y.Patskovsky, B.Hillerich, R.D.Seidel, W.D.Zencheck, R.Toro, H.J.Imker, F.M.Raushel, J.A.Gerlt, S.C.Almo, Enzyme Function Initiative (Efi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.53
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 101.203, 101.203, 65.614, 90.00, 90.00, 120.00
R / Rfree (%) 12 / 15.6

Other elements in 3rhg:

The structure of Crystal Structure of Amidohydrolase PMI1525 (Target Efi-500319) From Proteus Mirabilis HI4320 also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure of Amidohydrolase PMI1525 (Target Efi-500319) From Proteus Mirabilis HI4320 (pdb code 3rhg). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Crystal Structure of Amidohydrolase PMI1525 (Target Efi-500319) From Proteus Mirabilis HI4320, PDB code: 3rhg:

Arsenic binding site 1 out of 1 in 3rhg

Go back to Arsenic Binding Sites List in 3rhg
Arsenic binding site 1 out of 1 in the Crystal Structure of Amidohydrolase PMI1525 (Target Efi-500319) From Proteus Mirabilis HI4320


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 Amidohydrolase PMI1525 (Target Efi-500319) From Proteus Mirabilis HI4320 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As370

b:24.3
occ:1.00
AS A:CAC370 0.0 24.3 1.0
O2 A:CAC370 1.7 20.7 1.0
O1 A:CAC370 1.7 22.1 1.0
C1 A:CAC370 1.9 24.4 1.0
C2 A:CAC370 1.9 26.1 1.0
ZN A:ZN368 3.1 22.5 1.0
ZN A:ZN367 3.3 21.1 1.0
OH A:TYR126 3.6 22.8 1.0
OE2 A:GLU166 3.7 21.1 1.0
O1 A:UNL372 3.7 30.4 0.5
OD2 A:ASP294 3.8 20.4 1.0
C1 A:UNL372 3.9 25.4 0.5
OE1 A:GLU166 4.0 20.0 1.0
NE2 A:HIS25 4.1 17.5 1.0
CD A:GLU166 4.2 20.0 1.0
NE2 A:HIS229 4.2 18.0 1.0
OD1 A:ASP294 4.3 20.5 1.0
C2 A:UNL374 4.4 27.8 0.5
CZ A:TYR126 4.4 21.7 1.0
ND1 A:HIS199 4.5 19.0 1.0
CG A:ASP294 4.5 18.7 1.0
CE1 A:HIS229 4.5 18.7 1.0
C3 A:BEZ369 4.6 29.2 1.0
C2 A:BEZ369 4.6 30.6 1.0
CD1 A:PHE296 4.7 21.2 1.0
CE1 A:HIS199 4.7 22.8 1.0
CE1 A:TYR126 4.7 20.4 1.0
CG A:PHE296 4.7 19.6 1.0
CE1 A:HIS25 4.8 17.1 1.0
CD2 A:HIS25 4.9 18.1 1.0
C2 A:UNL372 4.9 26.8 0.5
O4 A:UNL373 4.9 29.1 0.5
CE1 A:PHE296 5.0 20.3 1.0

Reference:

Y.Patskovsky, B.Hillerich, R.D.Seidel, W.D.Zencheck, R.Toro, H.J.Imker, F.M.Raushel, J.A.Gerlt, S.C.Almo. Crystal Structure of Amidohydrolase PMI1525 From Proteus Mirabilis HI4320 To Be Published.
Page generated: Sat Dec 12 01:41:51 2020

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