Chlorine in PDB 5u0l: X-Ray Crystal Structure of Fatty Aldehyde Dehydrogenase Enzymes From Marinobacter Aquaeolei VT8 Complexed with A Substrate

Enzymatic activity of X-Ray Crystal Structure of Fatty Aldehyde Dehydrogenase Enzymes From Marinobacter Aquaeolei VT8 Complexed with A Substrate

All present enzymatic activity of X-Ray Crystal Structure of Fatty Aldehyde Dehydrogenase Enzymes From Marinobacter Aquaeolei VT8 Complexed with A Substrate:
1.2.1.71;

Protein crystallography data

The structure of X-Ray Crystal Structure of Fatty Aldehyde Dehydrogenase Enzymes From Marinobacter Aquaeolei VT8 Complexed with A Substrate, PDB code: 5u0l was solved by K.Shi, K.Mulliner, B.M.Barney, H.Aihara, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.90 / 2.29
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 98.710, 98.710, 254.725, 90.00, 90.00, 90.00
R / Rfree (%) 21.4 / 27

Chlorine Binding Sites:

The binding sites of Chlorine atom in the X-Ray Crystal Structure of Fatty Aldehyde Dehydrogenase Enzymes From Marinobacter Aquaeolei VT8 Complexed with A Substrate (pdb code 5u0l). 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 X-Ray Crystal Structure of Fatty Aldehyde Dehydrogenase Enzymes From Marinobacter Aquaeolei VT8 Complexed with A Substrate, PDB code: 5u0l:

Chlorine binding site 1 out of 1 in 5u0l

Go back to Chlorine Binding Sites List in 5u0l
Chlorine binding site 1 out of 1 in the X-Ray Crystal Structure of Fatty Aldehyde Dehydrogenase Enzymes From Marinobacter Aquaeolei VT8 Complexed with A Substrate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Crystal Structure of Fatty Aldehyde Dehydrogenase Enzymes From Marinobacter Aquaeolei VT8 Complexed with A Substrate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl503

b:0.7
occ:1.00
 O B:HOH616 3.1 70.0 1.0
NH2 B:ARG138 3.5 74.5 1.0
NH1 B:ARG138 3.5 78.9 1.0
CZ B:ARG138 3.9 73.6 1.0
CG B:ARG136 4.2 51.4 1.0
CG1 A:VAL423 4.7 57.0 1.0
CB B:ARG136 4.8 48.5 1.0
NE B:ARG136 4.9 57.5 1.0

Reference:

J.H.Bertram, K.M.Mulliner, K.Shi, M.H.Plunkett, P.Nixon, N.A.Serratore, C.J.Douglas, H.Aihara, B.M.Barney. Five Fatty Aldehyde Dehydrogenase Enzymes From Marinobacter and Acinetobacter Spp. and Structural Insights Into the Aldehyde Binding Pocket. Appl. Environ. Microbiol. V. 83 2017.
ISSN: ESSN 1098-5336
PubMed: 28389542
DOI: 10.1128/AEM.00018-17
Page generated: Sat Dec 12 12:29:53 2020

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