Xenon in PDB 1fo6: Crystal Structure Analysis of N-Carbamoyl-D-Amino-Acid Amidohydrolase

All present enzymatic activity of Crystal Structure Analysis of N-Carbamoyl-D-Amino-Acid Amidohydrolase:
3.4.22.12;

The structure of Crystal Structure Analysis of N-Carbamoyl-D-Amino-Acid Amidohydrolase, PDB code: 1fo6 was solved by W.-C.Wang, W.-H.Hsu, F.-T.Chien, C.-Y.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	70.230, 67.530, 137.480, 90.00, 96.12, 90.00
R / Rfree (%)	n/a / 23.9

The binding sites of Xenon atom in the Crystal Structure Analysis of N-Carbamoyl-D-Amino-Acid Amidohydrolase (pdb code 1fo6). This binding sites where shown within 5.0 Angstroms radius around Xenon atom.
In total 2 binding sites of Xenon where determined in the Crystal Structure Analysis of N-Carbamoyl-D-Amino-Acid Amidohydrolase, PDB code: 1fo6:
Jump to Xenon binding site number: 1; 2;

Xenon binding site 1 out of 2 in the Crystal Structure Analysis of N-Carbamoyl-D-Amino-Acid Amidohydrolase


Mono view


Stereo pair view

A full contact list of Xenon with other atoms in the Xe binding site number 1 of Crystal Structure Analysis of N-Carbamoyl-D-Amino-Acid Amidohydrolase within 5.0Å range: probe atom residue distance (Å) B Occ B:Xe1001 b:25.6 occ:1.00 CB B:PRO178 4.0 15.3 1.0 CG A:GLU179 4.0 17.2 1.0 CB A:PRO178 4.0 16.5 1.0 CG B:GLU179 4.1 20.1 1.0 N B:GLU179 4.1 16.2 1.0 C B:PRO178 4.1 15.7 1.0 CD1 A:ILE301 4.2 16.9 1.0 N A:GLU179 4.2 17.1 1.0 CD1 B:ILE301 4.2 17.8 1.0 C A:PRO178 4.2 17.9 1.0 CA B:GLU179 4.2 18.5 1.0 CG A:PRO178 4.2 17.2 1.0 CG B:PRO178 4.3 16.6 1.0 CA A:GLU179 4.3 16.2 1.0 CD A:GLU179 4.4 14.6 1.0 CD B:GLU179 4.4 20.9 1.0 O B:PRO178 4.4 16.3 1.0 O A:PRO178 4.5 16.7 1.0 CB B:ARG182 4.5 14.4 1.0 CB A:ARG182 4.6 15.6 1.0 CG2 A:ILE301 4.7 17.3 1.0 CB B:GLU179 4.7 17.7 1.0 CA B:PRO178 4.7 15.4 1.0 CA A:PRO178 4.8 16.8 1.0 OE1 B:GLU179 4.8 16.7 1.0 OE1 A:GLU179 4.8 13.3 1.0 CG2 B:ILE301 4.8 22.8 1.0 OE2 B:GLU179 4.8 20.7 1.0 CB A:GLU179 4.8 14.9 1.0 OE2 A:GLU179 4.9 15.6 1.0 CG B:ARG182 4.9 16.1 1.0

Xenon binding site 2 out of 2 in the Crystal Structure Analysis of N-Carbamoyl-D-Amino-Acid Amidohydrolase


Mono view


Stereo pair view

A full contact list of Xenon with other atoms in the Xe binding site number 2 of Crystal Structure Analysis of N-Carbamoyl-D-Amino-Acid Amidohydrolase within 5.0Å range: probe atom residue distance (Å) B Occ C:Xe1002 b:27.5 occ:1.00 CB D:PRO178 4.0 17.2 1.0 CB C:PRO178 4.0 16.9 1.0 CG C:GLU179 4.1 19.4 1.0 C C:PRO178 4.2 16.8 1.0 N C:GLU179 4.2 14.1 1.0 CG D:GLU179 4.2 19.5 1.0 CG C:PRO178 4.2 18.5 1.0 C D:PRO178 4.2 17.3 1.0 CD1 D:ILE301 4.2 21.6 1.0 N D:GLU179 4.3 15.0 1.0 CG D:PRO178 4.3 19.5 1.0 CA C:GLU179 4.3 16.4 1.0 O D:PRO178 4.4 15.5 1.0 CD1 C:ILE301 4.4 21.7 1.0 O C:PRO178 4.4 17.5 1.0 CA D:GLU179 4.4 17.9 1.0 CD C:GLU179 4.5 20.1 1.0 CD D:GLU179 4.5 20.3 1.0 CB C:ARG182 4.5 15.7 1.0 CG2 D:ILE301 4.6 23.4 1.0 CB D:ARG182 4.7 15.2 1.0 CA C:PRO178 4.7 14.5 1.0 CA D:PRO178 4.8 16.8 1.0 CG2 C:ILE301 4.8 22.4 1.0 OE1 C:GLU179 4.8 18.3 1.0 OE1 D:GLU179 4.8 21.0 1.0 CG C:ARG182 4.9 16.5 1.0 CB D:GLU179 4.9 16.7 1.0 CB C:GLU179 4.9 16.0 1.0 OE2 C:GLU179 4.9 20.6 1.0 OE2 D:GLU179 4.9 20.1 1.0

W.C.Wang, W.H.Hsu, F.T.Chien, C.Y.Chen. Crystal Structure and Site-Directed Mutagenesis Studies of N-Carbamoyl-D-Amino-Acid Amidohydrolase From Agrobacterium Radiobacter Reveals A Homotetramer and Insight Into A Catalytic Cleft. J.Mol.Biol. V. 306 251 2001.
ISSN: ISSN 0022-2836
PubMed: 11237598
DOI: 10.1006/JMBI.2000.4380