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Zinc in PDB 1wdk: Fatty Acid Beta-Oxidation Multienzyme Complex From Pseudomonas Fragi, Form I (NATIVE2)

Enzymatic activity of Fatty Acid Beta-Oxidation Multienzyme Complex From Pseudomonas Fragi, Form I (NATIVE2)

All present enzymatic activity of Fatty Acid Beta-Oxidation Multienzyme Complex From Pseudomonas Fragi, Form I (NATIVE2):
1.1.1.35; 2.3.1.16; 4.2.1.17; 5.1.2.3; 5.3.3.8;

Protein crystallography data

The structure of Fatty Acid Beta-Oxidation Multienzyme Complex From Pseudomonas Fragi, Form I (NATIVE2), PDB code: 1wdk was solved by M.Ishikawa, D.Tsuchiya, T.Oyama, Y.Tsunaka, K.Morikawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 180.705, 94.578, 160.001, 90.00, 111.45, 90.00
R / Rfree (%) 20.3 / 24.4

Other elements in 1wdk:

The structure of Fatty Acid Beta-Oxidation Multienzyme Complex From Pseudomonas Fragi, Form I (NATIVE2) also contains other interesting chemical elements:

Mercury (Hg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Fatty Acid Beta-Oxidation Multienzyme Complex From Pseudomonas Fragi, Form I (NATIVE2) (pdb code 1wdk). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Fatty Acid Beta-Oxidation Multienzyme Complex From Pseudomonas Fragi, Form I (NATIVE2), PDB code: 1wdk:

Zinc binding site 1 out of 1 in 1wdk

Go back to Zinc Binding Sites List in 1wdk
Zinc binding site 1 out of 1 in the Fatty Acid Beta-Oxidation Multienzyme Complex From Pseudomonas Fragi, Form I (NATIVE2)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Fatty Acid Beta-Oxidation Multienzyme Complex From Pseudomonas Fragi, Form I (NATIVE2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn716

b:43.2
occ:1.00
NE2 A:HIS550 2.1 45.4 1.0
CE1 A:HIS550 2.8 44.3 1.0
OD1 A:ASP573 3.2 48.8 1.0
CD2 A:HIS550 3.4 44.4 1.0
NH2 A:ARG553 4.0 60.6 1.0
ND1 A:HIS550 4.0 44.9 1.0
CG A:HIS550 4.3 44.2 1.0
CD2 A:TYR576 4.4 46.7 1.0
CG A:ASP573 4.4 47.5 1.0
OE2 A:GLU577 4.5 40.6 1.0
CE2 A:TYR576 4.8 47.8 1.0
CZ A:ARG553 5.0 60.9 1.0

Reference:

M.Ishikawa, D.Tsuchiya, T.Oyama, Y.Tsunaka, K.Morikawa. Structural Basis For Channelling Mechanism of A Fatty Acid Beta-Oxidation Multienzyme Complex Embo J. V. 23 2745 2004.
ISSN: ISSN 0261-4189
PubMed: 15229654
DOI: 10.1038/SJ.EMBOJ.7600298
Page generated: Wed Oct 16 19:58:37 2024

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