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Chlorine in PDB 1y56: Crystal Structure of L-Proline Dehydrogenase From P.Horikoshii

Enzymatic activity of Crystal Structure of L-Proline Dehydrogenase From P.Horikoshii

All present enzymatic activity of Crystal Structure of L-Proline Dehydrogenase From P.Horikoshii:
1.5.99.8;

Protein crystallography data

The structure of Crystal Structure of L-Proline Dehydrogenase From P.Horikoshii, PDB code: 1y56 was solved by H.Tsuge, R.Kawakami, H.Sakuraba, H.Ago, M.Miyano, K.Aki, N.Katunuma, T.Ohshima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.85 / 2.86
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 172.219, 172.219, 175.398, 90.00, 90.00, 120.00
R / Rfree (%) 18.2 / 22.6

Other elements in 1y56:

The structure of Crystal Structure of L-Proline Dehydrogenase From P.Horikoshii also contains other interesting chemical elements:

Iron (Fe) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of L-Proline Dehydrogenase From P.Horikoshii (pdb code 1y56). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of L-Proline Dehydrogenase From P.Horikoshii, PDB code: 1y56:

Chlorine binding site 1 out of 1 in 1y56

Go back to Chlorine Binding Sites List in 1y56
Chlorine binding site 1 out of 1 in the Crystal Structure of L-Proline Dehydrogenase From P.Horikoshii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of L-Proline Dehydrogenase From P.Horikoshii within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl804

b:25.2
occ:1.00
N B:GLY335 3.1 30.3 1.0
N B:ALA309 3.2 30.9 1.0
ND2 B:ASN202 3.2 26.7 1.0
O3' B:FAD800 3.2 21.7 1.0
N B:SER334 3.3 30.7 1.0
CA B:TYR308 3.7 30.7 1.0
C3' B:FAD800 3.7 22.9 1.0
C B:PHE333 3.8 30.9 1.0
CA B:GLY335 3.9 29.9 1.0
CA B:SER334 3.9 30.9 1.0
C B:TYR308 3.9 30.9 1.0
C B:SER334 4.0 30.6 1.0
C1' B:FAD800 4.0 23.6 1.0
O B:TYR307 4.1 30.6 1.0
CA B:ALA309 4.2 31.0 1.0
N B:PHE333 4.2 30.9 1.0
CA B:PHE333 4.2 30.9 1.0
CB B:PHE333 4.2 31.1 1.0
CB B:ALA309 4.3 30.7 1.0
O B:ALA309 4.4 31.6 1.0
O B:PHE333 4.4 30.7 1.0
CG B:ASN202 4.4 29.0 1.0
CB B:TYR308 4.5 30.6 1.0
C2' B:FAD800 4.5 23.3 1.0
C B:ALA309 4.6 31.5 1.0
C B:GLY335 4.6 29.9 1.0
CG B:TYR308 4.8 31.1 1.0
N B:TYR308 4.8 30.4 1.0
N B:HIS336 4.8 29.2 1.0
CD1 B:TYR308 4.8 31.5 1.0
C B:TYR307 4.8 30.5 1.0
C5' B:FAD800 4.9 23.0 1.0
OD1 B:ASN202 4.9 30.4 1.0
C4' B:FAD800 4.9 23.3 1.0

Reference:

H.Tsuge, R.Kawakami, H.Sakuraba, H.Ago, M.Miyano, K.Aki, N.Katunuma, T.Ohshima. Crystal Structure of A Novel Fad-, Fmn-, and Atp-Containing L-Proline Dehydrogenase Complex From Pyrococcus Horikoshii J.Biol.Chem. V. 280 31045 2005.
ISSN: ISSN 0021-9258
PubMed: 16027125
DOI: 10.1074/JBC.C500234200
Page generated: Sat Dec 12 08:55:10 2020

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