Copper in PDB 4z12: Recombinantly Expressed Latent Aurone Synthase (Polyphenol Oxidase) Co-Crystallized with Hexatungstotellurate(VI)

The structure of Recombinantly Expressed Latent Aurone Synthase (Polyphenol Oxidase) Co-Crystallized with Hexatungstotellurate(VI), PDB code: 4z12 was solved by C.Molitor, S.G.Mauracher, A.Rompel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.14 / 1.85
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.990, 110.410, 94.990, 90.00, 95.76, 90.00
R / Rfree (%)	17.2 / 20.5

The structure of Recombinantly Expressed Latent Aurone Synthase (Polyphenol Oxidase) Co-Crystallized with Hexatungstotellurate(VI) also contains other interesting chemical elements:

Tungsten	(W)	19 atoms
Tellurium	(Te)	3 atoms

The binding sites of Copper atom in the Recombinantly Expressed Latent Aurone Synthase (Polyphenol Oxidase) Co-Crystallized with Hexatungstotellurate(VI) (pdb code 4z12). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Recombinantly Expressed Latent Aurone Synthase (Polyphenol Oxidase) Co-Crystallized with Hexatungstotellurate(VI), PDB code: 4z12:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in the Recombinantly Expressed Latent Aurone Synthase (Polyphenol Oxidase) Co-Crystallized with Hexatungstotellurate(VI)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Recombinantly Expressed Latent Aurone Synthase (Polyphenol Oxidase) Co-Crystallized with Hexatungstotellurate(VI) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu601 b:48.5 occ:1.00 NE2 A:HIS96 2.0 40.3 1.0 NE2 A:HIS119 2.1 43.3 1.0 NE2 A:HIS128 2.1 35.2 1.0 O A:HOH863 2.3 50.4 1.0 CE1 A:HIS128 2.9 36.0 1.0 HE1 A:HIS128 2.9 43.2 1.0 CE1 A:HIS119 2.9 47.6 1.0 CD2 A:HIS96 3.0 36.6 1.0 CE1 A:HIS96 3.0 40.6 1.0 CD2 A:HIS119 3.2 44.6 1.0 HD2 A:HIS96 3.2 43.9 1.0 HE1 A:HIS96 3.2 48.7 1.0 CD2 A:HIS128 3.3 33.5 1.0 HD2 A:HIS119 3.4 53.6 1.0 SG A:CYS100 3.6 40.7 1.0 HD2 A:HIS128 3.6 40.2 1.0 HD11 A:ILE118 3.7 48.1 1.0 CU A:CU602 3.9 47.4 1.0 HZ A:PHE285 4.0 41.2 1.0 HE1 A:PHE285 4.0 39.5 1.0 HE1 A:HIS289 4.0 44.1 1.0 ND1 A:HIS128 4.1 31.9 1.0 ND1 A:HIS96 4.1 42.5 1.0 ND1 A:HIS119 4.1 46.3 1.0 CG A:HIS96 4.1 37.1 1.0 HE1 A:PHE124 4.1 39.4 1.0 NE2 A:HIS289 4.2 38.5 1.0 CG A:HIS119 4.2 45.1 1.0 CG A:HIS128 4.3 30.4 1.0 CE1 A:HIS289 4.3 36.8 1.0 HD1 A:PHE276 4.4 62.9 1.0 HE1 A:PHE276 4.5 66.0 1.0 CD1 A:PHE276 4.5 52.4 1.0 CE1 A:PHE276 4.5 55.0 1.0 CD1 A:ILE118 4.5 40.0 1.0 HE2 A:PHE127 4.6 41.3 1.0 CZ A:PHE285 4.7 34.4 1.0 CE1 A:PHE285 4.7 32.9 1.0 HD12 A:ILE118 4.7 48.1 1.0 HD1 A:PHE124 4.8 38.9 1.0 HD1 A:HIS128 4.8 38.3 1.0 HD13 A:ILE118 4.8 48.1 1.0 HD2 A:PHE127 4.8 39.6 1.0 CE1 A:PHE124 4.8 32.9 1.0 HD1 A:HIS119 4.9 55.6 1.0 HD1 A:HIS96 4.9 50.9 1.0 HE1 A:HIS255 4.9 46.2 1.0 NE2 A:HIS255 5.0 41.0 1.0

Copper binding site 2 out of 4 in the Recombinantly Expressed Latent Aurone Synthase (Polyphenol Oxidase) Co-Crystallized with Hexatungstotellurate(VI)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Recombinantly Expressed Latent Aurone Synthase (Polyphenol Oxidase) Co-Crystallized with Hexatungstotellurate(VI) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu602 b:47.4 occ:1.00 O A:HOH863 1.9 50.4 1.0 NE2 A:HIS255 2.0 41.0 1.0 NE2 A:HIS289 2.1 38.5 1.0 NE2 A:HIS259 2.1 50.9 1.0 CE1 A:HIS289 2.9 36.8 1.0 CD2 A:HIS255 2.9 33.8 1.0 HE1 A:HIS289 2.9 44.1 1.0 CE1 A:HIS255 3.0 38.5 1.0 CD2 A:HIS259 3.0 47.9 1.0 CE1 A:HIS259 3.1 50.9 1.0 HD2 A:HIS255 3.1 40.5 1.0 HD2 A:HIS259 3.2 57.5 1.0 HE1 A:HIS255 3.2 46.2 1.0 HE1 A:PHE285 3.2 39.5 1.0 CD2 A:HIS289 3.2 37.4 1.0 HE1 A:HIS259 3.3 61.1 1.0 HD2 A:HIS289 3.5 44.9 1.0 HE1 A:PHE276 3.8 66.0 1.0 CU A:CU601 3.9 48.5 1.0 HE1 A:PHE124 4.0 39.4 1.0 ND1 A:HIS255 4.0 38.5 1.0 CE1 A:PHE285 4.0 32.9 1.0 CG A:HIS255 4.1 37.0 1.0 ND1 A:HIS289 4.1 31.1 1.0 CG A:HIS259 4.1 45.2 1.0 ND1 A:HIS259 4.1 50.6 1.0 HD2 A:HIS288 4.2 44.2 1.0 CG A:HIS289 4.3 33.1 1.0 HD1 A:PHE285 4.4 40.8 1.0 CE1 A:PHE276 4.5 55.0 1.0 HZ A:PHE124 4.5 37.0 1.0 NE2 A:HIS96 4.6 40.3 1.0 HE1 A:HIS96 4.7 48.7 1.0 HE2 A:HIS288 4.7 44.2 1.0 HD1 A:PHE276 4.7 62.9 1.0 NE2 A:HIS128 4.7 35.2 1.0 CD1 A:PHE285 4.7 34.0 1.0 CE1 A:PHE124 4.8 32.9 1.0 HD1 A:HIS289 4.8 37.3 1.0 CD2 A:HIS288 4.8 36.8 1.0 HD1 A:HIS255 4.8 46.2 1.0 HD1 A:HIS259 4.9 60.7 1.0 HZ A:PHE285 4.9 41.2 1.0 CE1 A:HIS96 5.0 40.6 1.0 CZ A:PHE285 5.0 34.4 1.0

Copper binding site 3 out of 4 in the Recombinantly Expressed Latent Aurone Synthase (Polyphenol Oxidase) Co-Crystallized with Hexatungstotellurate(VI)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Recombinantly Expressed Latent Aurone Synthase (Polyphenol Oxidase) Co-Crystallized with Hexatungstotellurate(VI) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu601 b:45.3 occ:1.00 NE2 B:HIS96 1.9 37.9 1.0 NE2 B:HIS128 2.2 29.4 1.0 NE2 B:HIS119 2.2 38.7 1.0 O B:HOH733 2.6 49.5 1.0 CD2 B:HIS96 2.9 39.4 1.0 CE1 B:HIS96 2.9 37.8 1.0 CE1 B:HIS128 2.9 26.8 1.0 HE1 B:HIS128 3.0 32.2 1.0 CE1 B:HIS119 3.0 39.3 1.0 HD2 B:HIS96 3.1 47.3 1.0 HE1 B:HIS96 3.2 45.4 1.0 CD2 B:HIS128 3.3 27.1 1.0 CD2 B:HIS119 3.3 34.5 1.0 HD2 B:HIS119 3.5 41.4 1.0 SG B:CYS100 3.6 36.3 1.0 HD2 B:HIS128 3.6 32.5 1.0 HD11 B:ILE118 3.7 45.4 1.0 CU B:CU602 3.9 44.9 1.0 HZ B:PHE285 3.9 39.4 1.0 HE1 B:PHE285 4.0 37.8 1.0 ND1 B:HIS96 4.0 39.4 1.0 CG B:HIS96 4.1 38.5 1.0 HD1 B:PHE276 4.1 63.6 1.0 HE1 B:PHE276 4.1 61.7 1.0 ND1 B:HIS128 4.1 27.7 1.0 NE2 B:HIS289 4.2 35.0 1.0 HE1 B:HIS289 4.2 34.2 1.0 ND1 B:HIS119 4.2 38.8 1.0 CD1 B:PHE276 4.3 53.0 1.0 CE1 B:PHE276 4.3 51.4 1.0 HE1 B:PHE124 4.3 32.9 1.0 CG B:HIS128 4.3 23.5 1.0 CG B:HIS119 4.4 37.9 1.0 CE1 B:HIS289 4.4 28.5 1.0 CD1 B:ILE118 4.5 37.8 1.0 HE2 B:PHE127 4.5 30.0 1.0 CZ B:PHE285 4.6 32.8 1.0 CE1 B:PHE285 4.6 31.5 1.0 HD12 B:ILE118 4.6 45.4 1.0 HD13 B:ILE118 4.7 45.4 1.0 HD2 B:PHE127 4.8 33.0 1.0 HD1 B:HIS96 4.8 47.3 1.0 HD1 B:HIS128 4.9 33.2 1.0 HD1 B:HIS119 5.0 46.6 1.0 NE2 B:HIS255 5.0 30.8 1.0 HD1 B:PHE124 5.0 33.6 1.0

Copper binding site 4 out of 4 in the Recombinantly Expressed Latent Aurone Synthase (Polyphenol Oxidase) Co-Crystallized with Hexatungstotellurate(VI)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Recombinantly Expressed Latent Aurone Synthase (Polyphenol Oxidase) Co-Crystallized with Hexatungstotellurate(VI) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu602 b:44.9 occ:1.00 O B:HOH733 1.8 49.5 1.0 NE2 B:HIS289 2.1 35.0 1.0 NE2 B:HIS255 2.1 30.8 1.0 NE2 B:HIS259 2.1 52.0 1.0 CD2 B:HIS255 2.9 26.0 1.0 CE1 B:HIS289 3.0 28.5 1.0 HD2 B:HIS255 3.0 31.2 1.0 CD2 B:HIS259 3.0 50.3 1.0 CE1 B:HIS259 3.1 54.2 1.0 HE1 B:HIS289 3.1 34.2 1.0 CD2 B:HIS289 3.1 33.5 1.0 CE1 B:HIS255 3.1 33.9 1.0 HD2 B:HIS259 3.2 60.4 1.0 HE1 B:PHE285 3.2 37.8 1.0 HE1 B:HIS259 3.3 65.0 1.0 HD2 B:HIS289 3.3 40.1 1.0 HE1 B:HIS255 3.4 40.7 1.0 HE1 B:PHE276 3.8 61.7 1.0 CU B:CU601 3.9 45.3 1.0 HE1 B:PHE124 4.0 32.9 1.0 CE1 B:PHE285 4.0 31.5 1.0 HD2 B:HIS288 4.0 36.9 1.0 ND1 B:HIS289 4.1 27.6 1.0 CG B:HIS255 4.1 28.3 1.0 ND1 B:HIS259 4.1 53.3 1.0 CG B:HIS259 4.2 47.1 1.0 ND1 B:HIS255 4.2 33.0 1.0 CG B:HIS289 4.2 26.3 1.0 HD1 B:PHE285 4.5 38.8 1.0 HE2 B:HIS288 4.5 36.1 1.0 NE2 B:HIS128 4.6 29.4 1.0 HZ B:PHE124 4.6 30.4 1.0 CE1 B:PHE276 4.6 51.4 1.0 CD2 B:HIS288 4.7 30.8 1.0 CD1 B:PHE285 4.7 32.4 1.0 NE2 B:HIS96 4.7 37.9 1.0 HD1 B:PHE276 4.7 63.6 1.0 HE1 B:HIS96 4.7 45.4 1.0 CE1 B:PHE124 4.8 27.4 1.0 HD1 B:HIS289 4.9 33.2 1.0 HZ B:PHE285 4.9 39.4 1.0 NE2 B:HIS288 4.9 30.1 1.0 CZ B:PHE285 4.9 32.8 1.0 HD1 B:HIS259 4.9 64.0 1.0 HD1 B:HIS255 5.0 39.6 1.0 CD2 B:HIS128 5.0 27.1 1.0 CE1 B:HIS96 5.0 37.8 1.0

C.Molitor, S.G.Mauracher, A.Rompel. Aurone Synthase Is A Catechol Oxidase with Hydroxylase Activity and Provides Insights Into the Mechanism of Plant Polyphenol Oxidases. Proc.Natl.Acad.Sci.Usa V. 113 E1806 2016.
ISSN: ESSN 1091-6490
PubMed: 26976571
DOI: 10.1073/PNAS.1523575113