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Zinc 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:

Arsenic (As) 1 atom

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Amidohydrolase PMI1525 (Target Efi-500319) From Proteus Mirabilis HI4320, PDB code: 3rhg:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3rhg

Go back to Zinc Binding Sites List in 3rhg
Zinc binding site 1 out of 2 in the Crystal Structure of Amidohydrolase PMI1525 (Target Efi-500319) From Proteus Mirabilis HI4320


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn 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:Zn367

b:21.1
occ:1.00
O1 A:CAC370 1.9 22.1 1.0
NE2 A:HIS25 2.0 17.5 1.0
NE2 A:HIS23 2.1 18.1 1.0
OE2 A:GLU166 2.1 21.1 1.0
OD1 A:ASP294 2.4 20.5 1.0
CE1 A:HIS25 3.0 17.1 1.0
CD2 A:HIS25 3.0 18.1 1.0
CE1 A:HIS23 3.0 21.1 1.0
CD2 A:HIS23 3.1 17.9 1.0
CD A:GLU166 3.2 20.0 1.0
CG A:ASP294 3.2 18.7 1.0
AS A:CAC370 3.3 24.3 1.0
OD2 A:ASP294 3.5 20.4 1.0
OE1 A:GLU166 3.6 20.0 1.0
C2 A:CAC370 3.7 26.1 1.0
ZN A:ZN368 3.9 22.5 1.0
ND1 A:HIS25 4.1 18.4 1.0
CE1 A:HIS229 4.1 18.7 1.0
ND1 A:HIS23 4.1 19.0 1.0
O2 A:CAC370 4.1 20.7 1.0
CG A:HIS25 4.1 16.5 1.0
CG A:HIS23 4.2 19.3 1.0
NE2 A:HIS229 4.4 18.0 1.0
CG A:GLU166 4.5 19.7 1.0
CB A:ASP294 4.5 20.2 1.0
CB A:ALA95 4.6 17.2 1.0
C1 A:CAC370 4.8 24.4 1.0

Zinc binding site 2 out of 2 in 3rhg

Go back to Zinc Binding Sites List in 3rhg
Zinc binding site 2 out of 2 in the Crystal Structure of Amidohydrolase PMI1525 (Target Efi-500319) From Proteus Mirabilis HI4320


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 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:Zn368

b:22.5
occ:1.00
OE1 A:GLU166 1.9 20.0 1.0
O2 A:CAC370 1.9 20.7 1.0
ND1 A:HIS199 2.0 19.0 1.0
NE2 A:HIS229 2.0 18.0 1.0
CD A:GLU166 2.9 20.0 1.0
CE1 A:HIS199 2.9 22.8 1.0
O1 A:CAC370 3.0 22.1 1.0
CD2 A:HIS229 3.0 19.0 1.0
CE1 A:HIS229 3.0 18.7 1.0
AS A:CAC370 3.1 24.3 1.0
CG A:HIS199 3.1 17.9 1.0
OE2 A:GLU166 3.4 21.1 1.0
CB A:HIS199 3.5 17.8 1.0
ZN A:ZN367 3.9 21.1 1.0
OH A:TYR126 4.0 22.8 1.0
NE2 A:HIS199 4.1 22.7 1.0
CE1 A:TYR126 4.1 20.4 1.0
ND1 A:HIS229 4.1 20.1 1.0
CA A:HIS199 4.2 16.6 1.0
CG A:HIS229 4.2 18.7 1.0
CD2 A:HIS199 4.2 20.3 1.0
CG A:GLU166 4.2 19.7 1.0
C1 A:CAC370 4.4 24.4 1.0
C2 A:CAC370 4.5 26.1 1.0
CE1 A:HIS23 4.5 21.1 1.0
NE2 A:HIS23 4.6 18.1 1.0
CZ A:TYR126 4.6 21.7 1.0
C2 A:BEZ369 4.6 30.6 1.0
C3 A:BEZ369 4.9 29.2 1.0
CB A:GLU166 4.9 17.5 1.0
OD2 A:ASP294 4.9 20.4 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 Oct 26 14:48:31 2024

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