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Chlorine in PDB 3uha: Crystal Structure of Saccharopine Dehydrogenase From Saccharomyces Cervisiae Complexed with Nad.

Enzymatic activity of Crystal Structure of Saccharopine Dehydrogenase From Saccharomyces Cervisiae Complexed with Nad.

All present enzymatic activity of Crystal Structure of Saccharopine Dehydrogenase From Saccharomyces Cervisiae Complexed with Nad.:
1.5.1.7;

Protein crystallography data

The structure of Crystal Structure of Saccharopine Dehydrogenase From Saccharomyces Cervisiae Complexed with Nad., PDB code: 3uha was solved by P.F.Cook, V.P.Kumar, L.M.Thomas, A.H.West, K.D.Bobyk, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.64 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 64.010, 104.450, 69.080, 90.00, 116.60, 90.00
R / Rfree (%) 20.7 / 27

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Saccharopine Dehydrogenase From Saccharomyces Cervisiae Complexed with Nad. (pdb code 3uha). 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 Saccharopine Dehydrogenase From Saccharomyces Cervisiae Complexed with Nad., PDB code: 3uha:

Chlorine binding site 1 out of 1 in 3uha

Go back to Chlorine Binding Sites List in 3uha
Chlorine binding site 1 out of 1 in the Crystal Structure of Saccharopine Dehydrogenase From Saccharomyces Cervisiae Complexed with Nad.


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 Saccharopine Dehydrogenase From Saccharomyces Cervisiae Complexed with Nad. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl375

b:20.0
occ:1.00
N A:LYS193 3.2 12.2 1.0
CG A:ARG192 3.9 24.6 1.0
CA A:ARG192 3.9 15.4 1.0
CD A:LYS193 3.9 18.6 1.0
CB A:LYS193 3.9 11.3 1.0
CG A:LYS193 3.9 14.7 1.0
C A:ARG192 4.0 13.6 1.0
CA A:LYS193 4.1 12.2 1.0
CB A:ARG192 4.5 16.5 1.0
CE A:LYS193 4.8 21.1 1.0
O A:LYS193 4.9 11.2 1.0

Reference:

V.P.Kumar, L.M.Thomas, K.D.Bobyk, B.Andi, P.F.Cook, A.H.West. Evidence in Support of Lysine 77 and Histidine 96 As Acid-Base Catalytic Residues in Saccharopine Dehydrogenase From Saccharomyces Cerevisiae. Biochemistry V. 51 857 2012.
ISSN: ISSN 0006-2960
PubMed: 22243403
DOI: 10.1021/BI201808U
Page generated: Sat Dec 12 10:14:56 2020

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