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Chlorine in PDB 7dl0: The Mutant E310G/A314Y of 3,5-Dahdhcca Complex with Nadph

Enzymatic activity of The Mutant E310G/A314Y of 3,5-Dahdhcca Complex with Nadph

All present enzymatic activity of The Mutant E310G/A314Y of 3,5-Dahdhcca Complex with Nadph:
1.4.1.11;

Protein crystallography data

The structure of The Mutant E310G/A314Y of 3,5-Dahdhcca Complex with Nadph, PDB code: 7dl0 was solved by N.Liu, L.Wu, D.M.Zhu, J.H.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.56 / 2.17
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 161.882, 161.882, 125.69, 90, 90, 90
R / Rfree (%) 21.1 / 26.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Mutant E310G/A314Y of 3,5-Dahdhcca Complex with Nadph (pdb code 7dl0). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the The Mutant E310G/A314Y of 3,5-Dahdhcca Complex with Nadph, PDB code: 7dl0:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 7dl0

Go back to Chlorine Binding Sites List in 7dl0
Chlorine binding site 1 out of 2 in the The Mutant E310G/A314Y of 3,5-Dahdhcca Complex with Nadph


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Mutant E310G/A314Y of 3,5-Dahdhcca Complex with Nadph within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl405

b:55.3
occ:1.00
CE A:LYS190 4.3 50.1 1.0

Chlorine binding site 2 out of 2 in 7dl0

Go back to Chlorine Binding Sites List in 7dl0
Chlorine binding site 2 out of 2 in the The Mutant E310G/A314Y of 3,5-Dahdhcca Complex with Nadph


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of The Mutant E310G/A314Y of 3,5-Dahdhcca Complex with Nadph within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl406

b:69.8
occ:1.00
OD2 A:ASP49 2.5 82.6 1.0
O A:GLY94 2.8 81.7 1.0
CG A:ASP49 3.7 84.6 1.0
OG A:SER125 3.7 64.7 1.0
C A:GLY94 3.9 78.9 1.0
N A:GLY94 3.9 73.6 1.0
CB A:SER125 4.3 56.3 1.0
CA A:GLY94 4.5 77.4 1.0
CB A:SER93 4.5 77.0 1.0
OD1 A:ASP49 4.5 85.3 1.0
CB A:ASP49 4.6 78.1 1.0
CD1 B:LEU307 4.7 46.8 1.0
CA A:SER93 4.8 69.3 1.0
N A:GLY95 4.8 70.0 1.0
C A:SER93 4.8 70.8 1.0
CA A:GLY95 4.9 66.8 1.0
O A:HOH581 5.0 51.1 1.0

Reference:

N.Liu, L.Wu, J.Feng, X.Sheng, J.Li, X.Chen, J.Li, W.Liu, J.Zhou, Q.Wu, D.Zhu. Crystal Structures and Catalytic Mechanism of L-Erythro-3,5-Diaminohexanoate Dehydrogenase and Rational Engineering For Asymmetric Synthesis of Beta-Amino Acids. Angew.Chem.Int.Ed.Engl. V. 60 10203 2021.
ISSN: ESSN 1521-3773
PubMed: 33624917
DOI: 10.1002/ANIE.202017225
Page generated: Sun Jul 13 00:07:53 2025

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