Zinc in PDB 3eef: Crystal Structure of N-Carbamoylsarcosine Amidase From Thermoplasma Acidophilum

All present enzymatic activity of Crystal Structure of N-Carbamoylsarcosine Amidase From Thermoplasma Acidophilum:
3.5.1.59;

The structure of Crystal Structure of N-Carbamoylsarcosine Amidase From Thermoplasma Acidophilum, PDB code: 3eef was solved by H.-B.Luo, H.Zheng, M.Chruszcz, M.D.Zimmerman, T.Skarina, O.Egorova, A.Savchenko, A.Joachimiak, W.Minor, Midwest Center For Structuralgenomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.85 / 2.35
Space group	P 62
Cell size a, b, c (Å), α, β, γ (°)	83.970, 83.970, 98.725, 90.00, 90.00, 120.00
R / Rfree (%)	19.4 / 24.1

The binding sites of Zinc atom in the Crystal Structure of N-Carbamoylsarcosine Amidase From Thermoplasma Acidophilum (pdb code 3eef). 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 N-Carbamoylsarcosine Amidase From Thermoplasma Acidophilum, PDB code: 3eef:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of N-Carbamoylsarcosine Amidase From Thermoplasma Acidophilum


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 N-Carbamoylsarcosine Amidase From Thermoplasma Acidophilum within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn183 b:44.3 occ:0.50 OE1 A:GLU58 2.0 44.5 1.0 OD2 A:ASP50 2.0 59.7 1.0 NE2 A:HIS65 2.2 55.5 1.0 NE2 A:HIS52 2.2 47.9 1.0 CD A:GLU58 3.0 48.5 1.0 CG A:ASP50 3.0 49.6 1.0 CE1 A:HIS65 3.1 51.8 1.0 CD2 A:HIS52 3.2 37.6 1.0 CD2 A:HIS65 3.2 56.7 1.0 CE1 A:HIS52 3.2 44.9 1.0 OD1 A:ASP50 3.5 52.8 1.0 OE2 A:GLU58 3.6 40.3 1.0 CG A:GLU58 4.0 44.8 1.0 CB A:ASP50 4.1 45.5 1.0 ND1 A:HIS65 4.3 52.7 1.0 ND1 A:HIS52 4.3 44.7 1.0 CG A:HIS52 4.3 43.8 1.0 CG A:HIS65 4.3 55.5 1.0 CE1 A:TYR93 4.9 33.8 1.0 CD1 A:TYR93 4.9 39.5 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of N-Carbamoylsarcosine Amidase From Thermoplasma Acidophilum


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 N-Carbamoylsarcosine Amidase From Thermoplasma Acidophilum within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn183 b:55.7 occ:0.30 OD2 B:ASP50 2.0 60.1 1.0 OE1 B:GLU58 2.0 44.9 1.0 NE2 B:HIS65 2.2 55.3 1.0 NE2 B:HIS52 2.2 47.8 1.0 CG B:ASP50 2.9 49.6 1.0 O A:HOH190 3.0 61.2 1.0 CD B:GLU58 3.1 48.7 1.0 CD2 B:HIS52 3.1 37.1 1.0 CD2 B:HIS65 3.1 56.9 1.0 CE1 B:HIS65 3.1 52.2 1.0 CE1 B:HIS52 3.2 45.5 1.0 OD1 B:ASP50 3.4 52.5 1.0 OE2 B:GLU58 3.7 39.5 1.0 CB B:ASP50 3.9 45.3 1.0 CG B:GLU58 4.1 44.8 1.0 ND1 B:HIS65 4.2 53.4 1.0 CG B:HIS65 4.2 55.4 1.0 CG B:HIS52 4.2 43.3 1.0 ND1 B:HIS52 4.3 45.2 1.0 CZ B:PHE14 4.7 72.5 1.0

H.B.Luo, H.Zheng, M.D.Zimmerman, M.Chruszcz, T.Skarina, O.Egorova, A.Savchenko, A.M.Edwards, W.Minor. Crystal Structure and Molecular Modeling Study of N-Carbamoylsarcosine Amidase TA0454 From Thermoplasma Acidophilum. J.Struct.Biol. V. 169 304 2010.
ISSN: ISSN 1047-8477
PubMed: 19932181
DOI: 10.1016/J.JSB.2009.11.008