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Zinc in PDB 5ehf: Laccase From Antrodiella Faginea

Enzymatic activity of Laccase From Antrodiella Faginea

All present enzymatic activity of Laccase From Antrodiella Faginea:
1.10.3.2;

Protein crystallography data

The structure of Laccase From Antrodiella Faginea, PDB code: 5ehf was solved by K.M.Polyakov, O.A.Glazunova, T.V.Fedorova, P.V.Dorovatovskii, O.V.Koroleva, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 75.91 / 1.75
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 48.150, 81.540, 78.500, 90.00, 104.75, 90.00
R / Rfree (%) 16 / 19.5

Other elements in 5ehf:

The structure of Laccase From Antrodiella Faginea also contains other interesting chemical elements:

Copper (Cu) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Laccase From Antrodiella Faginea (pdb code 5ehf). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Laccase From Antrodiella Faginea, PDB code: 5ehf:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5ehf

Go back to Zinc Binding Sites List in 5ehf
Zinc binding site 1 out of 2 in the Laccase From Antrodiella Faginea


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Laccase From Antrodiella Faginea within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn511

b:23.7
occ:1.00
OD2 A:ASP366 1.9 23.7 1.0
ND1 A:HIS362 2.1 26.2 1.0
O A:HOH945 2.2 11.4 1.0
OD1 A:ASP366 2.4 18.2 1.0
CG A:ASP366 2.5 21.1 1.0
CE1 A:HIS362 2.9 24.7 1.0
CG A:HIS362 3.2 28.1 1.0
CB A:HIS362 3.7 25.9 1.0
N A:HIS362 3.9 24.1 1.0
CB A:ASP366 4.1 19.9 1.0
NE2 A:HIS362 4.1 28.3 1.0
CD2 A:HIS362 4.2 27.2 1.0
CA A:HIS362 4.4 23.7 1.0

Zinc binding site 2 out of 2 in 5ehf

Go back to Zinc Binding Sites List in 5ehf
Zinc binding site 2 out of 2 in the Laccase From Antrodiella Faginea


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Laccase From Antrodiella Faginea within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn512

b:21.2
occ:0.25
OD2 A:ASP167 1.9 25.5 1.0
O A:HOH891 2.1 31.9 1.0
CG A:ASP167 2.8 26.0 1.0
OD1 A:ASP167 3.1 30.2 1.0
N A:HIS153 3.5 16.9 1.0
N A:THR154 3.9 19.3 1.0
OG1 A:THR154 4.1 22.4 1.0
CB A:HIS153 4.1 20.4 1.0
CA A:HIS153 4.2 18.0 1.0
CB A:ASP167 4.2 21.5 1.0
C A:HIS153 4.5 19.8 1.0
O A:THR165 4.5 23.9 1.0
C A:TYR152 4.5 17.4 1.0
CB A:THR154 4.5 21.6 1.0
CA A:TYR152 4.6 16.9 1.0
CG A:HIS153 4.8 22.3 1.0
N A:ASP167 4.8 21.3 1.0
CA A:THR154 4.9 21.0 1.0
CA A:ASP167 4.9 20.6 1.0
CB A:TYR152 4.9 18.4 1.0
OE2 A:GLU159 5.0 28.4 1.0

Reference:

O.A.Glazunova, K.M.Polyakov, K.V.Moiseenko, S.A.Kurzeev, T.V.Fedorova. Structure-Function Study of Two New Middle-Redox Potential Laccases From Basidiomycetes Antrodiella Faginea and Steccherinum Murashkinskyi. Int. J. Biol. Macromol. V. 118 406 2018.
ISSN: ISSN 1879-0003
PubMed: 29890251
DOI: 10.1016/J.IJBIOMAC.2018.06.038
Page generated: Sun Oct 27 15:21:34 2024

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