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Chlorine in PDB 5d2h: 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium and Alpha-Ketoglutarate

Enzymatic activity of 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium and Alpha-Ketoglutarate

All present enzymatic activity of 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium and Alpha-Ketoglutarate:
4.1.1.77;

Protein crystallography data

The structure of 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium and Alpha-Ketoglutarate, PDB code: 5d2h was solved by S.L.Guimaraes, R.A.P.Nagem, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.27 / 1.94
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.741, 44.904, 125.318, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 23.1

Other elements in 5d2h:

The structure of 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium and Alpha-Ketoglutarate also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium and Alpha-Ketoglutarate (pdb code 5d2h). 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 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium and Alpha-Ketoglutarate, PDB code: 5d2h:

Chlorine binding site 1 out of 1 in 5d2h

Go back to Chlorine Binding Sites List in 5d2h
Chlorine binding site 1 out of 1 in the 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium and Alpha-Ketoglutarate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of 4-Oxalocrotonate Decarboxylase From Pseudomonas Putida G7 - Complexed with Magnesium and Alpha-Ketoglutarate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl312

b:26.2
occ:1.00
O A:HOH458 3.0 26.8 1.0
NE A:ARG167 3.1 19.7 1.0
N A:ASP99 3.2 16.1 1.0
NH2 A:ARG167 3.4 16.9 1.0
CZ A:ARG167 3.7 17.7 1.0
CB A:ASP99 3.8 15.7 1.0
CA A:ASP99 4.0 16.2 1.0
O A:HOH551 4.0 31.1 1.0
O A:ASP99 4.1 14.7 1.0
CA A:VAL98 4.1 16.9 1.0
C A:VAL98 4.2 15.8 1.0
CD A:LYS102 4.2 28.0 1.0
CG1 A:VAL98 4.2 13.4 1.0
CD A:ARG167 4.3 16.0 1.0
C A:ASP99 4.5 18.3 1.0
O A:VAL97 4.6 15.4 1.0
O A:HOH473 4.7 21.0 1.0
CB A:LYS102 4.8 16.2 1.0
CB A:VAL98 4.8 17.2 1.0
CG A:LYS102 4.9 15.7 1.0

Reference:

S.L.Guimaraes, J.B.Coitinho, D.M.Costa, S.S.Araujo, C.P.Whitman, R.A.Nagem. Crystal Structures of Apo and Liganded 4-Oxalocrotonate Decarboxylase Uncover A Structural Basis For the Metal-Assisted Decarboxylation of A Vinylogous Beta-Keto Acid. Biochemistry V. 55 2632 2016.
ISSN: ISSN 0006-2960
PubMed: 27082660
DOI: 10.1021/ACS.BIOCHEM.6B00050
Page generated: Fri Jul 26 06:29:42 2024

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