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

Enzymatic activity of 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;

Protein crystallography data

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

Xenon Binding Sites:

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 1fo6

Go back to Xenon Binding Sites List in 1fo6
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 1fo6

Go back to Xenon Binding Sites List in 1fo6
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

Reference:

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
Page generated: Wed Dec 16 02:39:20 2020

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