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Copper in PDB 1bt3: Catechol Oxidase From Ipomoea Batatas (Sweet Potatoes) in the Native Cu(II)-Cu(II) State

Enzymatic activity of Catechol Oxidase From Ipomoea Batatas (Sweet Potatoes) in the Native Cu(II)-Cu(II) State

All present enzymatic activity of Catechol Oxidase From Ipomoea Batatas (Sweet Potatoes) in the Native Cu(II)-Cu(II) State:
1.10.3.1;

Protein crystallography data

The structure of Catechol Oxidase From Ipomoea Batatas (Sweet Potatoes) in the Native Cu(II)-Cu(II) State, PDB code: 1bt3 was solved by T.Klabunde, C.Eicken, J.C.Sacchettini, B.Krebs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.50
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 46.120, 156.750, 56.070, 90.00, 90.00, 90.00
R / Rfree (%) 16.7 / 25

Copper Binding Sites:

The binding sites of Copper atom in the Catechol Oxidase From Ipomoea Batatas (Sweet Potatoes) in the Native Cu(II)-Cu(II) State (pdb code 1bt3). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Catechol Oxidase From Ipomoea Batatas (Sweet Potatoes) in the Native Cu(II)-Cu(II) State, PDB code: 1bt3:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1bt3

Go back to Copper Binding Sites List in 1bt3
Copper binding site 1 out of 2 in the Catechol Oxidase From Ipomoea Batatas (Sweet Potatoes) in the Native Cu(II)-Cu(II) State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Catechol Oxidase From Ipomoea Batatas (Sweet Potatoes) in the Native Cu(II)-Cu(II) State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu500

b:15.7
occ:1.00
CU2 A:C2O500 0.0 15.7 1.0
O1 A:C2O500 1.9 16.2 1.0
NE2 A:HIS88 2.2 11.2 1.0
NE2 A:HIS118 2.3 8.3 1.0
NE2 A:HIS109 2.3 16.0 1.0
CU3 A:C2O500 2.9 17.9 1.0
CD2 A:HIS109 3.1 16.5 1.0
CE1 A:HIS88 3.1 11.3 1.0
CE1 A:HIS118 3.1 9.5 1.0
CD2 A:HIS88 3.2 6.2 1.0
CD2 A:HIS118 3.3 6.6 1.0
CE1 A:HIS109 3.5 14.1 1.0
NE2 A:HIS274 3.9 17.2 1.0
SG A:CYS92 4.1 11.8 1.0
CE1 A:HIS274 4.1 21.2 1.0
ND1 A:HIS88 4.2 6.9 1.0
ND1 A:HIS118 4.3 8.9 1.0
CG A:HIS109 4.3 15.1 1.0
CG A:HIS88 4.3 4.3 1.0
CE2 A:PHE270 4.4 4.8 1.0
NE2 A:HIS240 4.4 11.9 1.0
CG A:HIS118 4.4 6.5 1.0
ND1 A:HIS109 4.5 15.9 1.0
CZ A:PHE270 4.5 2.0 1.0
NE2 A:HIS244 4.6 10.4 1.0
CD1 A:PHE261 4.7 12.3 1.0
CE1 A:PHE261 4.8 13.7 1.0
CE1 A:PHE114 4.8 3.6 1.0
CG A:PHE261 4.8 12.6 1.0
CZ A:PHE261 4.9 13.2 1.0
CD2 A:HIS274 4.9 16.6 1.0
CE1 A:HIS240 4.9 15.1 1.0
CD2 A:PHE261 4.9 14.2 1.0
CE2 A:PHE261 4.9 10.9 1.0

Copper binding site 2 out of 2 in 1bt3

Go back to Copper Binding Sites List in 1bt3
Copper binding site 2 out of 2 in the Catechol Oxidase From Ipomoea Batatas (Sweet Potatoes) in the Native Cu(II)-Cu(II) State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Catechol Oxidase From Ipomoea Batatas (Sweet Potatoes) in the Native Cu(II)-Cu(II) State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu500

b:17.9
occ:1.00
CU3 A:C2O500 0.0 17.9 1.0
O1 A:C2O500 1.8 16.2 1.0
NE2 A:HIS240 2.1 11.9 1.0
NE2 A:HIS244 2.2 10.4 1.0
NE2 A:HIS274 2.2 17.2 1.0
CU2 A:C2O500 2.9 15.7 1.0
CE1 A:HIS240 3.0 15.1 1.0
CD2 A:HIS240 3.1 14.5 1.0
CE1 A:HIS274 3.1 21.2 1.0
CD2 A:HIS244 3.2 7.9 1.0
CE1 A:HIS244 3.2 10.2 1.0
CD2 A:HIS274 3.3 16.6 1.0
ND1 A:HIS240 4.1 15.1 1.0
NE2 A:HIS118 4.2 8.3 1.0
CG A:HIS240 4.2 13.5 1.0
ND1 A:HIS274 4.3 18.4 1.0
ND1 A:HIS244 4.3 7.6 1.0
CG A:HIS244 4.3 8.2 1.0
CG A:HIS274 4.4 15.9 1.0
CE2 A:PHE270 4.4 4.8 1.0
CE1 A:PHE261 4.4 13.7 1.0
NE2 A:HIS88 4.4 11.2 1.0
CE1 A:PHE114 4.4 3.6 1.0
CD2 A:HIS118 4.7 6.6 1.0
NE2 A:HIS109 4.7 16.0 1.0
CZ A:PHE261 4.8 13.2 1.0
CE1 A:HIS118 4.8 9.5 1.0
CD2 A:HIS109 4.8 16.5 1.0
CZ A:PHE114 4.8 3.8 1.0
CE1 A:HIS88 4.8 11.3 1.0
CD1 A:PHE261 5.0 12.3 1.0
O A:HOH505 5.0 21.9 1.0

Reference:

T.Klabunde, C.Eicken, J.C.Sacchettini, B.Krebs. Crystal Structure of A Plant Catechol Oxidase Containing A Dicopper Center. Nat.Struct.Biol. V. 5 1084 1998.
ISSN: ISSN 1072-8368
PubMed: 9846879
DOI: 10.1038/4193
Page generated: Sun Dec 13 10:58:11 2020

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