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Cobalt in PDB 6w54: Crystal Structure of Gallic Acid Decarboxylase From Arxula Adeninivorans

Protein crystallography data

The structure of Crystal Structure of Gallic Acid Decarboxylase From Arxula Adeninivorans, PDB code: 6w54 was solved by M.Zeug, N.Marckovic, C.V.Iancu, J.Tripp, M.Oreb, J.Choe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.70 / 1.50
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 81.971, 81.971, 103.055, 90, 90, 120
R / Rfree (%) 14 / 16.6

Other elements in 6w54:

The structure of Crystal Structure of Gallic Acid Decarboxylase From Arxula Adeninivorans also contains other interesting chemical elements:

Potassium (K) 1 atom

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of Gallic Acid Decarboxylase From Arxula Adeninivorans (pdb code 6w54). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystal Structure of Gallic Acid Decarboxylase From Arxula Adeninivorans, PDB code: 6w54:

Cobalt binding site 1 out of 1 in 6w54

Go back to Cobalt Binding Sites List in 6w54
Cobalt binding site 1 out of 1 in the Crystal Structure of Gallic Acid Decarboxylase From Arxula Adeninivorans


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of Gallic Acid Decarboxylase From Arxula Adeninivorans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co303

b:22.3
occ:1.00
O A:HOH466 2.0 30.8 1.0
OE1 A:GLU49 2.0 19.4 1.0
O A:HOH410 2.2 27.1 1.0
O A:HOH519 2.3 31.8 1.0
CD A:GLU49 3.0 20.1 1.0
OE2 A:GLU49 3.4 22.9 1.0
OD1 A:ASN46 4.2 22.3 1.0
CG A:GLU49 4.4 18.0 1.0
CB A:GLU49 4.7 15.9 1.0

Reference:

M.Zeug, N.Markovic, C.V.Iancu, J.Tripp, M.Oreb, J.Y.Choe. Crystal Structures of Non-Oxidative Decarboxylases Reveal A New Mechanism of Action with A Catalytic Dyad and Structural Twists. Sci Rep V. 11 3056 2021.
ISSN: ESSN 2045-2322
PubMed: 33542397
DOI: 10.1038/S41598-021-82660-Z
Page generated: Wed Mar 3 13:04:02 2021

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