Atomistry » Copper » PDB 4yst-5c14 » 4z0z
Atomistry »
  Copper »
    PDB 4yst-5c14 »
      4z0z »

Copper in PDB 4z0z: Inactive Aurone Synthase (Polyphenol Oxidase) From Natural Source, Sulfohistidine ~ 90 %

Protein crystallography data

The structure of Inactive Aurone Synthase (Polyphenol Oxidase) From Natural Source, Sulfohistidine ~ 90 %, PDB code: 4z0z 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) 48.10 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.530, 183.520, 78.090, 90.00, 94.50, 90.00
R / Rfree (%) 16.5 / 20

Copper Binding Sites:

The binding sites of Copper atom in the Inactive Aurone Synthase (Polyphenol Oxidase) From Natural Source, Sulfohistidine ~ 90 % (pdb code 4z0z). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Inactive Aurone Synthase (Polyphenol Oxidase) From Natural Source, Sulfohistidine ~ 90 %, PDB code: 4z0z:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 4z0z

Go back to Copper Binding Sites List in 4z0z
Copper binding site 1 out of 4 in the Inactive Aurone Synthase (Polyphenol Oxidase) From Natural Source, Sulfohistidine ~ 90 %


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Inactive Aurone Synthase (Polyphenol Oxidase) From Natural Source, Sulfohistidine ~ 90 % within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu700

b:17.6
occ:1.00
NE2 A:HIS93 2.0 12.7 1.0
NE2 A:HIS125 2.0 16.0 1.0
NE2 A:HIS116 2.0 14.4 1.0
CE1 A:HIS125 2.8 17.3 1.0
HE1 A:HIS125 2.9 20.7 1.0
CD2 A:HIS93 2.9 12.7 1.0
CE1 A:HIS93 3.0 14.1 1.0
O1 A:HS8252 3.0 24.9 0.9
CE1 A:HIS116 3.0 11.7 1.0
CD2 A:HIS116 3.1 13.3 1.0
HD2 A:HIS93 3.1 15.3 1.0
CD2 A:HIS125 3.1 15.8 1.0
HE1 A:HIS93 3.2 16.9 1.0
HD2 A:HIS116 3.3 16.0 1.0
HD11 A:ILE115 3.3 20.2 1.0
HD2 A:HIS125 3.4 18.9 1.0
SG A:CYS97 3.5 13.2 1.0
HE2 A:HIS286 3.7 28.9 1.0
O2 A:HS8252 3.8 29.4 0.9
S A:HS8252 3.9 22.8 0.9
ND1 A:HIS125 4.0 15.1 1.0
ND1 A:HIS93 4.0 12.7 1.0
CG A:HIS93 4.0 11.3 1.0
CD1 A:ILE115 4.1 16.8 1.0
HZ A:PHE282 4.1 20.5 1.0
ND1 A:HIS116 4.1 14.2 1.0
CG A:HIS116 4.2 14.2 1.0
HD12 A:ILE115 4.2 20.2 1.0
CG A:HIS125 4.2 15.6 1.0
HE1 A:PHE282 4.3 13.2 1.0
HD13 A:ILE115 4.3 20.2 1.0
NE2 A:HIS286 4.3 24.1 1.0
HE1 A:PHE121 4.4 19.7 1.0
HE2 A:PHE124 4.4 14.8 1.0
HD1 A:PHE273 4.6 22.6 1.0
HD2 A:PHE124 4.7 12.8 1.0
HD1 A:HIS125 4.7 18.1 1.0
HD1 A:HIS93 4.8 15.2 1.0
O3 A:HS8252 4.8 23.6 0.9
CZ A:PHE282 4.8 17.1 1.0
CD1 A:PHE273 4.8 18.8 1.0
HD1 A:HIS116 4.9 17.0 1.0
HD1 A:PHE121 4.9 19.6 1.0
CE1 A:PHE282 4.9 11.0 1.0
CD2 A:HIS286 5.0 17.9 1.0

Copper binding site 2 out of 4 in 4z0z

Go back to Copper Binding Sites List in 4z0z
Copper binding site 2 out of 4 in the Inactive Aurone Synthase (Polyphenol Oxidase) From Natural Source, Sulfohistidine ~ 90 %


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Inactive Aurone Synthase (Polyphenol Oxidase) From Natural Source, Sulfohistidine ~ 90 % within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu700

b:15.8
occ:1.00
NE2 B:HIS125 1.9 11.8 1.0
NE2 B:HIS93 2.0 10.8 1.0
NE2 B:HIS116 2.1 12.5 1.0
CE1 B:HIS125 2.8 13.7 1.0
CD2 B:HIS93 2.8 12.7 1.0
HE1 B:HIS125 3.0 16.4 1.0
CE1 B:HIS93 3.0 12.5 1.0
HD2 B:HIS93 3.0 15.3 1.0
CD2 B:HIS116 3.0 12.6 1.0
O2 B:HS8252 3.0 24.0 0.9
CD2 B:HIS125 3.0 12.4 1.0
CE1 B:HIS116 3.1 11.3 1.0
HD2 B:HIS116 3.2 15.1 1.0
HE1 B:HIS93 3.2 15.0 1.0
HD2 B:HIS125 3.3 14.8 1.0
HD11 B:ILE115 3.4 16.4 1.0
O3 B:HS8252 3.4 25.6 0.9
SG B:CYS97 3.5 10.8 1.0
HE2 B:HIS286 3.7 23.7 1.0
S B:HS8252 3.8 21.1 0.9
HZ B:PHE282 3.9 20.2 1.0
ND1 B:HIS125 4.0 13.7 1.0
CG B:HIS93 4.0 9.8 1.0
ND1 B:HIS93 4.0 13.5 1.0
CG B:HIS125 4.1 12.4 1.0
CD1 B:ILE115 4.2 13.7 1.0
CG B:HIS116 4.2 13.6 1.0
ND1 B:HIS116 4.2 11.9 1.0
HE1 B:PHE282 4.3 22.3 1.0
HD12 B:ILE115 4.3 16.4 1.0
NE2 B:HIS286 4.3 19.8 1.0
HD13 B:ILE115 4.3 16.4 1.0
HE1 B:PHE121 4.4 16.5 1.0
HE2 B:PHE124 4.4 14.8 1.0
HD1 B:PHE273 4.6 19.1 1.0
HD2 B:PHE124 4.6 13.9 1.0
O1 B:HS8252 4.7 19.6 0.9
CZ B:PHE282 4.7 16.8 1.0
HD1 B:HIS125 4.8 16.4 1.0
HD1 B:HIS93 4.8 16.2 1.0
CD1 B:PHE273 4.8 15.9 1.0
CE1 B:PHE282 4.9 18.6 1.0
HD1 B:PHE121 4.9 13.9 1.0
HD2 B:HIS286 4.9 19.8 1.0
HB3 B:PHE273 4.9 14.2 1.0
CD2 B:HIS286 5.0 16.5 1.0
HD1 B:HIS116 5.0 14.3 1.0

Copper binding site 3 out of 4 in 4z0z

Go back to Copper Binding Sites List in 4z0z
Copper binding site 3 out of 4 in the Inactive Aurone Synthase (Polyphenol Oxidase) From Natural Source, Sulfohistidine ~ 90 %


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Inactive Aurone Synthase (Polyphenol Oxidase) From Natural Source, Sulfohistidine ~ 90 % within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu700

b:17.3
occ:1.00
NE2 C:HIS93 1.9 14.0 1.0
NE2 C:HIS125 2.0 12.4 1.0
NE2 C:HIS116 2.1 13.8 1.0
CE1 C:HIS125 2.8 16.9 1.0
HE1 C:HIS125 2.8 20.3 1.0
CD2 C:HIS93 2.8 16.2 1.0
CE1 C:HIS93 2.9 16.7 1.0
HD2 C:HIS93 3.0 19.5 1.0
CE1 C:HIS116 3.0 14.1 1.0
CD2 C:HIS116 3.0 14.8 1.0
O1 C:HS8252 3.2 24.4 0.9
CD2 C:HIS125 3.2 14.9 1.0
HE1 C:HIS93 3.2 20.1 1.0
HD2 C:HIS116 3.2 17.8 1.0
HD11 C:ILE115 3.3 17.1 1.0
HD2 C:HIS125 3.5 17.8 1.0
SG C:CYS97 3.5 13.7 1.0
HE2 C:HIS286 3.6 27.3 1.0
HZ C:PHE282 3.8 20.4 1.0
S C:HS8252 4.0 21.5 0.9
ND1 C:HIS125 4.0 14.7 1.0
CG C:HIS93 4.0 11.9 1.0
ND1 C:HIS93 4.0 15.1 1.0
O3 C:HS8252 4.1 27.0 0.9
CD1 C:ILE115 4.1 14.3 1.0
ND1 C:HIS116 4.1 14.7 1.0
CG C:HIS116 4.1 15.4 1.0
HE1 C:PHE282 4.2 15.9 1.0
CG C:HIS125 4.2 12.7 1.0
HD12 C:ILE115 4.2 17.1 1.0
NE2 C:HIS286 4.3 22.8 1.0
HD13 C:ILE115 4.3 17.1 1.0
HE2 C:PHE124 4.4 14.9 1.0
HD1 C:PHE273 4.5 25.3 1.0
CZ C:PHE282 4.6 17.0 1.0
HD2 C:PHE124 4.6 13.7 1.0
HE1 C:PHE121 4.7 21.5 1.0
HD1 C:HIS125 4.7 17.7 1.0
HD1 C:HIS93 4.8 18.1 1.0
CE1 C:PHE282 4.8 13.2 1.0
HD1 C:HIS116 4.9 17.6 1.0
CD1 C:PHE273 4.9 21.1 1.0
HB3 C:PHE273 4.9 15.2 1.0
HE1 C:HIS286 4.9 24.5 1.0
CE1 C:HIS286 4.9 20.4 1.0
O2 C:HS8252 5.0 25.2 0.9
HD1 C:PHE121 5.0 17.4 1.0

Copper binding site 4 out of 4 in 4z0z

Go back to Copper Binding Sites List in 4z0z
Copper binding site 4 out of 4 in the Inactive Aurone Synthase (Polyphenol Oxidase) From Natural Source, Sulfohistidine ~ 90 %


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Inactive Aurone Synthase (Polyphenol Oxidase) From Natural Source, Sulfohistidine ~ 90 % within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cu700

b:15.4
occ:1.00
NE2 D:HIS93 1.9 7.9 1.0
NE2 D:HIS125 2.0 11.8 1.0
NE2 D:HIS116 2.0 9.2 1.0
CE1 D:HIS125 2.8 13.2 1.0
CD2 D:HIS93 2.9 8.9 1.0
HE1 D:HIS125 2.9 15.9 1.0
CE1 D:HIS93 2.9 12.5 1.0
CE1 D:HIS116 3.0 10.4 1.0
CD2 D:HIS116 3.0 9.3 1.0
O1 D:HS8252 3.0 18.6 0.9
HD2 D:HIS93 3.1 10.7 1.0
HE1 D:HIS93 3.1 15.0 1.0
CD2 D:HIS125 3.2 10.4 1.0
HD2 D:HIS116 3.2 11.2 1.0
HD11 D:ILE115 3.4 12.9 1.0
HD2 D:HIS125 3.5 12.4 1.0
O3 D:HS8252 3.5 24.8 0.9
SG D:CYS97 3.5 11.5 1.0
HE1 D:HIS286 3.8 27.3 1.0
S D:HS8252 3.9 20.0 0.9
HZ D:PHE282 3.9 18.1 1.0
ND1 D:HIS93 4.0 13.0 1.0
CG D:HIS93 4.0 10.8 1.0
ND1 D:HIS125 4.0 11.4 1.0
ND1 D:HIS116 4.1 11.3 1.0
CG D:HIS116 4.1 8.3 1.0
CG D:HIS125 4.2 11.3 1.0
CD1 D:ILE115 4.2 10.7 1.0
HE1 D:PHE282 4.3 16.0 1.0
HD12 D:ILE115 4.3 12.9 1.0
HD13 D:ILE115 4.4 12.9 1.0
CE1 D:HIS286 4.4 22.7 1.0
HE2 D:PHE124 4.5 13.2 1.0
HD1 D:PHE273 4.5 16.6 1.0
HE1 D:PHE121 4.5 13.1 1.0
O2 D:HS8252 4.7 19.3 0.9
HD2 D:PHE124 4.7 11.7 1.0
CZ D:PHE282 4.7 15.1 1.0
HD1 D:HIS125 4.7 13.7 1.0
CD1 D:PHE273 4.8 13.8 1.0
HD1 D:HIS93 4.8 15.6 1.0
CE1 D:PHE282 4.9 13.3 1.0
HD1 D:HIS116 4.9 13.5 1.0
HB3 D:PHE273 4.9 12.9 1.0
HD1 D:PHE121 5.0 12.3 1.0

Reference:

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
Page generated: Sun Dec 13 11:16:38 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy