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Copper in PDB 2oqe: Crystal Structure of Hansenula Polymorpha Amine Oxidase in Complex with Xe to 1.6 Angstroms

Enzymatic activity of Crystal Structure of Hansenula Polymorpha Amine Oxidase in Complex with Xe to 1.6 Angstroms

All present enzymatic activity of Crystal Structure of Hansenula Polymorpha Amine Oxidase in Complex with Xe to 1.6 Angstroms:
1.4.3.6;

Protein crystallography data

The structure of Crystal Structure of Hansenula Polymorpha Amine Oxidase in Complex with Xe to 1.6 Angstroms, PDB code: 2oqe was solved by B.J.Johnson, C.M.Wilmot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.68 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 103.403, 222.751, 103.651, 90.00, 95.85, 90.00
R / Rfree (%) 16.2 / 18.8

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Hansenula Polymorpha Amine Oxidase in Complex with Xe to 1.6 Angstroms (pdb code 2oqe). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the Crystal Structure of Hansenula Polymorpha Amine Oxidase in Complex with Xe to 1.6 Angstroms, PDB code: 2oqe:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 2oqe

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Copper binding site 1 out of 6 in the Crystal Structure of Hansenula Polymorpha Amine Oxidase in Complex with Xe to 1.6 Angstroms


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Hansenula Polymorpha Amine Oxidase in Complex with Xe to 1.6 Angstroms within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu801

b:17.3
occ:1.00
NE2 A:HIS458 2.0 14.5 1.0
ND1 A:HIS624 2.1 16.3 1.0
NE2 A:HIS456 2.1 13.9 1.0
O A:HOH4062 2.9 26.9 1.0
CD2 A:HIS456 2.9 12.6 1.0
CD2 A:HIS458 3.0 14.4 1.0
CG A:HIS624 3.0 14.8 1.0
CE1 A:HIS458 3.0 15.0 1.0
CE1 A:HIS624 3.1 17.6 1.0
CE1 A:HIS456 3.1 15.5 1.0
CB A:HIS624 3.3 13.4 1.0
CG A:HIS456 4.1 13.1 1.0
CG A:HIS458 4.1 13.0 1.0
ND1 A:HIS458 4.1 13.5 1.0
CD2 A:HIS624 4.2 15.8 1.0
ND1 A:HIS456 4.2 12.7 1.0
NE2 A:HIS624 4.2 13.5 1.0
O A:HOH4057 4.6 18.5 1.0
CD1 A:ILE622 4.7 21.9 1.0
CA A:HIS624 4.8 12.7 1.0
OE A:SME634 4.8 32.1 1.0
O2 A:TPQ405 4.8 27.9 1.0
CD1 A:LEU425 4.8 23.5 1.0
O A:HOH4160 5.0 37.4 1.0

Copper binding site 2 out of 6 in 2oqe

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Copper binding site 2 out of 6 in the Crystal Structure of Hansenula Polymorpha Amine Oxidase in Complex with Xe to 1.6 Angstroms


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Hansenula Polymorpha Amine Oxidase in Complex with Xe to 1.6 Angstroms within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu801

b:17.3
occ:1.00
NE2 B:HIS458 2.0 13.2 1.0
ND1 B:HIS624 2.0 16.1 1.0
NE2 B:HIS456 2.1 14.3 1.0
O B:HOH4195 2.9 26.6 1.0
CD2 B:HIS456 2.9 13.7 1.0
CG B:HIS624 3.0 13.6 1.0
CE1 B:HIS458 3.0 14.1 1.0
CD2 B:HIS458 3.0 13.4 1.0
CE1 B:HIS624 3.1 15.7 1.0
CE1 B:HIS456 3.1 13.6 1.0
CB B:HIS624 3.3 13.2 1.0
CG B:HIS456 4.1 13.0 1.0
ND1 B:HIS458 4.1 11.7 1.0
ND1 B:HIS456 4.1 14.0 1.0
CD2 B:HIS624 4.2 15.3 1.0
NE2 B:HIS624 4.2 13.3 1.0
CG B:HIS458 4.2 11.5 1.0
O B:HOH4114 4.6 19.0 1.0
CA B:HIS624 4.8 12.0 1.0
CD1 B:ILE622 4.9 20.9 1.0
OE B:SME634 4.9 32.0 1.0
O2 B:TPQ405 4.9 29.8 1.0
CD1 B:LEU425 4.9 24.0 1.0

Copper binding site 3 out of 6 in 2oqe

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Copper binding site 3 out of 6 in the Crystal Structure of Hansenula Polymorpha Amine Oxidase in Complex with Xe to 1.6 Angstroms


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of Hansenula Polymorpha Amine Oxidase in Complex with Xe to 1.6 Angstroms within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu801

b:16.4
occ:1.00
ND1 C:HIS624 2.0 15.2 1.0
NE2 C:HIS458 2.0 10.4 1.0
NE2 C:HIS456 2.1 14.0 1.0
O4 C:TPQ405 2.9 21.9 0.3
CD2 C:HIS458 2.9 13.0 1.0
CG C:HIS624 2.9 15.3 1.0
CD2 C:HIS456 3.0 14.5 1.0
CE1 C:HIS624 3.0 16.8 1.0
CE1 C:HIS458 3.0 15.3 1.0
CE1 C:HIS456 3.1 13.6 1.0
CB C:HIS624 3.2 14.2 1.0
C4 C:TPQ405 3.5 19.1 0.3
C3 C:TPQ405 3.9 18.8 0.3
CD2 C:HIS624 4.1 15.7 1.0
CG C:HIS458 4.1 10.4 1.0
NE2 C:HIS624 4.1 14.0 1.0
ND1 C:HIS458 4.1 12.7 1.0
CG C:HIS456 4.1 13.4 1.0
ND1 C:HIS456 4.2 12.3 1.0
C5 C:TPQ405 4.5 18.3 0.3
O C:HOH4113 4.6 16.3 1.0
CA C:HIS624 4.7 12.7 1.0
CD1 C:LEU425 4.7 24.7 1.0
O5 C:TPQ405 4.8 18.1 0.3
CD1 C:ILE622 4.9 20.2 1.0
O2 C:TPQ405 5.0 29.2 0.7
CE C:MET634 5.0 27.7 1.0

Copper binding site 4 out of 6 in 2oqe

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Copper binding site 4 out of 6 in the Crystal Structure of Hansenula Polymorpha Amine Oxidase in Complex with Xe to 1.6 Angstroms


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of Hansenula Polymorpha Amine Oxidase in Complex with Xe to 1.6 Angstroms within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cu801

b:16.4
occ:1.00
NE2 D:HIS458 2.0 10.8 1.0
ND1 D:HIS624 2.0 15.4 1.0
NE2 D:HIS456 2.1 14.3 1.0
O4 D:TPQ405 2.9 19.3 0.4
CG D:HIS624 3.0 13.6 1.0
CD2 D:HIS458 3.0 13.6 1.0
CD2 D:HIS456 3.0 13.6 1.0
CE1 D:HIS458 3.0 13.2 1.0
CE1 D:HIS624 3.1 16.3 1.0
CE1 D:HIS456 3.1 14.8 1.0
CB D:HIS624 3.2 12.9 1.0
C4 D:TPQ405 3.5 16.6 0.4
C3 D:TPQ405 4.0 17.4 0.4
ND1 D:HIS458 4.1 13.3 1.0
CD2 D:HIS624 4.1 13.8 1.0
CG D:HIS458 4.1 11.4 1.0
NE2 D:HIS624 4.1 13.6 1.0
CG D:HIS456 4.2 13.0 1.0
ND1 D:HIS456 4.2 12.8 1.0
C5 D:TPQ405 4.4 17.0 0.4
O D:HOH4058 4.6 15.8 1.0
O2 D:TPQ405 4.6 24.9 0.6
O5 D:TPQ405 4.6 17.1 0.4
CA D:HIS624 4.8 13.1 1.0
CD1 D:ILE622 4.8 21.5 1.0

Copper binding site 5 out of 6 in 2oqe

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Copper binding site 5 out of 6 in the Crystal Structure of Hansenula Polymorpha Amine Oxidase in Complex with Xe to 1.6 Angstroms


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Crystal Structure of Hansenula Polymorpha Amine Oxidase in Complex with Xe to 1.6 Angstroms within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cu801

b:16.3
occ:1.00
ND1 E:HIS624 2.0 15.0 1.0
NE2 E:HIS458 2.0 11.4 1.0
NE2 E:HIS456 2.1 14.0 1.0
O4 E:TPQ405 2.9 20.9 0.4
CD2 E:HIS458 2.9 14.6 1.0
CG E:HIS624 3.0 12.6 1.0
CD2 E:HIS456 3.0 13.1 1.0
CE1 E:HIS624 3.0 14.5 1.0
CE1 E:HIS458 3.0 14.3 1.0
CE1 E:HIS456 3.1 14.6 1.0
CB E:HIS624 3.2 12.2 1.0
C4 E:TPQ405 3.5 17.8 0.4
CD2 E:LEU425 3.6 15.7 0.5
C3 E:TPQ405 3.9 18.6 0.4
CD2 E:HIS624 4.1 15.1 1.0
NE2 E:HIS624 4.1 13.5 1.0
CG E:HIS458 4.1 12.2 1.0
ND1 E:HIS458 4.1 12.9 1.0
CG E:HIS456 4.1 12.6 1.0
ND1 E:HIS456 4.1 13.9 1.0
C5 E:TPQ405 4.4 17.6 0.4
O E:HOH4054 4.6 14.8 1.0
O2 E:TPQ405 4.7 24.3 0.6
O5 E:TPQ405 4.7 18.5 0.4
CA E:HIS624 4.8 13.0 1.0
CD1 E:ILE622 4.8 21.2 1.0
CD1 E:LEU425 4.8 16.6 0.5
CG E:LEU425 5.0 15.7 0.5

Copper binding site 6 out of 6 in 2oqe

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Copper binding site 6 out of 6 in the Crystal Structure of Hansenula Polymorpha Amine Oxidase in Complex with Xe to 1.6 Angstroms


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Crystal Structure of Hansenula Polymorpha Amine Oxidase in Complex with Xe to 1.6 Angstroms within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cu801

b:16.5
occ:1.00
ND1 F:HIS624 2.0 14.7 1.0
NE2 F:HIS458 2.0 11.0 1.0
NE2 F:HIS456 2.1 13.0 1.0
O4 F:TPQ405 2.9 21.8 0.4
CD2 F:HIS458 2.9 12.6 1.0
CG F:HIS624 2.9 14.3 1.0
CD2 F:HIS456 3.0 13.5 1.0
CE1 F:HIS624 3.0 17.4 1.0
CE1 F:HIS458 3.1 13.7 1.0
CE1 F:HIS456 3.1 14.1 1.0
CB F:HIS624 3.2 13.3 1.0
C4 F:TPQ405 3.6 18.7 0.4
C3 F:TPQ405 4.0 19.1 0.4
CD2 F:HIS624 4.1 14.6 1.0
CG F:HIS458 4.1 12.3 1.0
NE2 F:HIS624 4.1 13.9 1.0
ND1 F:HIS458 4.1 13.5 1.0
CG F:HIS456 4.2 12.7 1.0
ND1 F:HIS456 4.2 12.7 1.0
C5 F:TPQ405 4.5 18.4 0.4
O F:HOH4149 4.6 15.9 1.0
O2 F:TPQ405 4.7 24.8 0.6
O5 F:TPQ405 4.7 18.5 0.4
CD1 F:LEU425 4.7 25.1 1.0
CA F:HIS624 4.8 12.6 1.0
CE F:MET634 4.8 28.4 1.0
CD1 F:ILE622 4.9 21.6 1.0

Reference:

B.J.Johnson, J.Cohen, R.W.Welford, A.R.Pearson, K.Schulten, J.P.Klinman, C.M.Wilmot. Exploring Molecular Oxygen Pathways in Hansenula Polymorpha Copper-Containing Amine Oxidase J.Biol.Chem. V. 282 17767 2007.
ISSN: ISSN 0021-9258
PubMed: 17409383
DOI: 10.1074/JBC.M701308200
Page generated: Thu Sep 3 16:46:16 2020
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