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Chlorine in PDB 5lww: Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc

Enzymatic activity of Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc

All present enzymatic activity of Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc:
1.10.3.2;

Protein crystallography data

The structure of Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc, PDB code: 5lww was solved by M.Ferraroni, F.Briganti, J.A.Tamayo-Ramos, W.J.H.Van Berkel, A.H.Westphal, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.65
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 88.446, 128.158, 134.676, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 26.7

Other elements in 5lww:

The structure of Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc also contains other interesting chemical elements:

Potassium (K) 1 atom
Zinc (Zn) 8 atoms
Copper (Cu) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc (pdb code 5lww). 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 Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc, PDB code: 5lww:

Chlorine binding site 1 out of 1 in 5lww

Go back to Chlorine Binding Sites List in 5lww
Chlorine binding site 1 out of 1 in the Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of A Laccase-Like Multicopper Oxidase Mcog From Aspergillus Niger Bound to Zinc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl625

b:48.3
occ:1.00
 ZN A:ZN616 2.9 39.5 1.0
CG A:PRO207 3.9 41.4 1.0
O A:HOH905 3.9 38.8 1.0
CA A:PRO207 4.1 42.5 1.0
NE2 A:HIS253 4.1 41.3 1.0
CZ2 A:TRP392 4.1 31.7 1.0
CB A:PRO207 4.1 40.0 1.0
NE2 A:HIS521 4.2 29.7 1.0
O A:HOH884 4.3 10.2 1.0
N A:PRO207 4.3 42.8 1.0
CD A:PRO207 4.4 42.2 1.0
CE1 A:HIS253 4.4 41.4 1.0
O A:GLN205 4.5 45.3 1.0
CG1 A:VAL446 4.7 34.6 1.0
CE1 A:HIS521 4.7 31.6 1.0
NE1 A:TRP392 4.8 31.7 1.0
CE2 A:TRP392 4.8 32.2 1.0
C A:ASN206 4.9 40.9 1.0
CE2 A:PHE381 4.9 41.0 1.0

Reference:

M.Ferraroni, A.H.Westphal, M.Borsari, J.A.Tamayo-Ramos, F.Briganti, L.H.De Graaff, W.J.H.Van Berkel. Structure and Function of Aspergillus Niger Laccase Mcog Biocatalysis 2017.
ISSN: ESSN 2353-1746
DOI: 10.1515/BOCA-2017-0001
Page generated: Sat Dec 12 12:04:35 2020

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