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Copper in PDB 4kfe: Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 7.0

Enzymatic activity of Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 7.0

All present enzymatic activity of Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 7.0:
1.4.3.21;

Protein crystallography data

The structure of Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 7.0, PDB code: 4kfe was solved by B.J.Johnson, E.T.Yukl, V.J.Klema, C.M.Wilmot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.03 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 103.577, 222.836, 103.619, 90.00, 95.87, 90.00
R / Rfree (%) 12.9 / 18

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 7.0 (pdb code 4kfe). 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 Copper Amine Oxidase-1 Reduced By Methylamine at pH 7.0, PDB code: 4kfe:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 4kfe

Go back to Copper Binding Sites List in 4kfe
Copper binding site 1 out of 6 in the Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 7.0


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 Copper Amine Oxidase-1 Reduced By Methylamine at pH 7.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu801

b:19.6
occ:1.00
ND1 A:HIS624 2.0 16.9 1.0
NE2 A:HIS456 2.1 14.5 1.0
NE2 A:HIS458 2.1 18.0 1.0
O1 A:PEO802 2.6 20.0 1.0
O2 A:PEO802 2.6 14.5 1.0
CE1 A:HIS624 2.9 18.7 1.0
CD2 A:HIS458 3.0 15.9 1.0
CD2 A:HIS456 3.0 14.6 1.0
CG A:HIS624 3.1 17.5 1.0
CE1 A:HIS456 3.1 15.1 1.0
CE1 A:HIS458 3.2 16.5 1.0
CB A:HIS624 3.4 15.8 1.0
NE2 A:HIS624 4.1 17.8 1.0
CD2 A:HIS624 4.2 17.3 1.0
CG A:HIS456 4.2 14.4 1.0
ND1 A:HIS456 4.2 15.2 1.0
CG A:HIS458 4.2 15.1 1.0
ND1 A:HIS458 4.2 15.4 1.0
O A:HOH1055 4.4 22.2 1.0
OZ A:TYY405 4.7 20.1 1.0
O A:HOH1193 4.9 40.4 1.0
CE A:MET634 4.9 29.3 1.0
CA A:HIS624 4.9 14.5 1.0
CD1 A:ILE622 5.0 25.5 1.0
CD2 A:LEU429 5.0 17.1 1.0

Copper binding site 2 out of 6 in 4kfe

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Copper binding site 2 out of 6 in the Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 7.0


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 Copper Amine Oxidase-1 Reduced By Methylamine at pH 7.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu801

b:20.6
occ:1.00
ND1 B:HIS624 2.0 19.6 1.0
NE2 B:HIS456 2.1 16.8 1.0
O2 B:PEO802 2.1 21.2 1.0
NE2 B:HIS458 2.1 16.3 1.0
O1 B:PEO802 2.9 13.0 1.0
CE1 B:HIS624 2.9 20.6 1.0
CG B:HIS624 3.0 19.1 1.0
CD2 B:HIS456 3.0 15.8 1.0
CE1 B:HIS456 3.1 16.6 1.0
CE1 B:HIS458 3.1 14.4 1.0
CD2 B:HIS458 3.1 14.3 1.0
CB B:HIS624 3.4 16.9 1.0
NE2 B:HIS624 4.0 20.2 1.0
CD2 B:HIS624 4.1 19.4 1.0
ND1 B:HIS456 4.2 16.2 1.0
CG B:HIS456 4.2 15.6 1.0
ND1 B:HIS458 4.2 15.0 1.0
CG B:HIS458 4.3 14.6 1.0
O B:HOH1094 4.4 21.3 1.0
O B:HOH1497 4.5 56.7 1.0
OZ B:TYY405 4.7 21.5 1.0
O B:HOH1179 4.8 34.2 1.0
CD1 B:LEU425 4.9 34.4 1.0
CA B:HIS624 5.0 14.7 1.0
CE B:MET634 5.0 33.0 1.0

Copper binding site 3 out of 6 in 4kfe

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Copper binding site 3 out of 6 in the Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 7.0


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 Copper Amine Oxidase-1 Reduced By Methylamine at pH 7.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu801

b:19.4
occ:1.00
ND1 C:HIS624 2.1 16.5 1.0
NE2 C:HIS458 2.1 18.9 1.0
NE2 C:HIS456 2.1 14.0 1.0
O2 C:PEO802 2.4 17.7 1.0
O1 C:PEO802 2.8 14.2 1.0
CE1 C:HIS624 3.0 16.7 1.0
CD2 C:HIS456 3.0 13.5 1.0
O C:HOH1426 3.0 50.4 1.0
CD2 C:HIS458 3.0 16.6 1.0
CG C:HIS624 3.1 15.2 1.0
CE1 C:HIS458 3.1 17.8 1.0
CE1 C:HIS456 3.2 13.5 1.0
CB C:HIS624 3.4 15.4 1.0
NE2 C:HIS624 4.1 15.7 1.0
CD2 C:HIS624 4.2 16.5 1.0
ND1 C:HIS458 4.2 17.4 1.0
CG C:HIS458 4.2 16.2 1.0
CG C:HIS456 4.2 13.6 1.0
ND1 C:HIS456 4.2 13.4 1.0
O C:HOH990 4.5 12.2 1.0
OZ C:TYY405 4.7 23.0 1.0
O C:HOH1120 4.7 43.4 1.0
CD1 C:LEU425 4.8 38.1 1.0
CA C:HIS624 4.9 14.1 1.0

Copper binding site 4 out of 6 in 4kfe

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Copper binding site 4 out of 6 in the Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 7.0


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 Copper Amine Oxidase-1 Reduced By Methylamine at pH 7.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cu703

b:20.2
occ:1.00
ND1 D:HIS624 2.1 17.1 1.0
NE2 D:HIS458 2.1 16.6 1.0
NE2 D:HIS456 2.2 13.9 1.0
O2 D:PEO701 2.7 17.9 1.0
O1 D:PEO701 2.7 17.6 1.0
CE1 D:HIS624 3.0 16.9 1.0
O D:HOH1351 3.0 39.1 1.0
CD2 D:HIS458 3.0 15.8 1.0
CD2 D:HIS456 3.1 14.6 1.0
CG D:HIS624 3.1 16.5 1.0
CE1 D:HIS458 3.1 15.9 1.0
CE1 D:HIS456 3.2 15.5 1.0
CB D:HIS624 3.5 16.6 1.0
NE2 D:HIS624 4.1 16.9 1.0
CD2 D:HIS624 4.2 16.7 1.0
ND1 D:HIS458 4.2 16.2 1.0
CG D:HIS458 4.2 14.7 1.0
CG D:HIS456 4.2 14.6 1.0
ND1 D:HIS456 4.3 15.0 1.0
O D:HOH805 4.5 13.1 1.0
OZ D:TYY405 4.7 25.0 1.0
O D:HOH1268 4.7 43.5 1.0
CD1 D:LEU425 4.8 32.5 1.0
CE D:MET634 5.0 31.9 1.0
CA D:HIS624 5.0 16.0 1.0

Copper binding site 5 out of 6 in 4kfe

Go back to Copper Binding Sites List in 4kfe
Copper binding site 5 out of 6 in the Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 7.0


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 Copper Amine Oxidase-1 Reduced By Methylamine at pH 7.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cu801

b:20.1
occ:1.00
NE2 E:HIS458 2.1 16.5 1.0
ND1 E:HIS624 2.1 16.3 1.0
NE2 E:HIS456 2.2 14.9 1.0
O2 E:PEO802 2.6 14.3 1.0
O1 E:PEO802 2.9 20.1 1.0
O E:HOH1432 2.9 40.9 1.0
CD2 E:HIS458 2.9 14.2 1.0
CD2 E:HIS456 3.0 13.6 1.0
CE1 E:HIS624 3.1 15.7 1.0
CG E:HIS624 3.1 15.6 1.0
CE1 E:HIS458 3.1 14.3 1.0
CE1 E:HIS456 3.3 15.7 1.0
CB E:HIS624 3.4 14.8 1.0
CG E:HIS458 4.1 14.2 1.0
ND1 E:HIS458 4.2 15.1 1.0
CG E:HIS456 4.2 14.2 1.0
NE2 E:HIS624 4.2 15.1 1.0
CD2 E:HIS624 4.3 15.3 1.0
ND1 E:HIS456 4.3 15.5 1.0
O E:HOH903 4.5 11.2 1.0
OZ E:TYY405 4.7 20.0 1.0
CD1 E:LEU425 4.7 35.0 1.0
CD1 E:ILE622 4.9 25.3 1.0
CA E:HIS624 4.9 14.2 1.0
SD E:MET634 5.0 46.4 1.0

Copper binding site 6 out of 6 in 4kfe

Go back to Copper Binding Sites List in 4kfe
Copper binding site 6 out of 6 in the Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 7.0


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 Copper Amine Oxidase-1 Reduced By Methylamine at pH 7.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cu801

b:19.2
occ:1.00
ND1 F:HIS624 2.1 16.0 1.0
NE2 F:HIS458 2.1 16.2 1.0
NE2 F:HIS456 2.1 15.6 1.0
O2 F:PEO802 2.3 16.4 1.0
O F:HOH1395 2.9 41.0 1.0
O1 F:PEO802 2.9 13.9 1.0
CD2 F:HIS456 3.0 15.0 1.0
CE1 F:HIS624 3.0 16.2 1.0
CD2 F:HIS458 3.0 15.4 1.0
CG F:HIS624 3.1 14.7 1.0
CE1 F:HIS458 3.2 17.2 1.0
CE1 F:HIS456 3.2 15.6 1.0
CB F:HIS624 3.4 13.9 1.0
NE2 F:HIS624 4.1 15.7 1.0
CD2 F:HIS624 4.2 15.8 1.0
CG F:HIS456 4.2 15.1 1.0
CG F:HIS458 4.2 16.3 1.0
ND1 F:HIS456 4.2 15.8 1.0
ND1 F:HIS458 4.2 17.2 1.0
O F:HOH983 4.5 11.8 1.0
OZ F:TYY405 4.6 21.8 1.0
CD1 F:LEU425 4.9 33.9 1.0
CD1 F:ILE622 4.9 26.1 1.0
CA F:HIS624 4.9 13.6 1.0
O F:HOH1077 4.9 36.6 1.0

Reference:

B.J.Johnson, E.T.Yukl, V.J.Klema, J.P.Klinman, C.M.Wilmot. Structural Evidence For the Semiquinone in A Copper Amine Oxidase From Hansenula Polymorpha: Implications For the Catalytic Mechanism J.Biol.Chem. 2013.
ISSN: ESSN 1083-351X
Page generated: Mon Jul 14 03:48:40 2025

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