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Copper in PDB 3loy: Crystal Structure of A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha

Enzymatic activity of Crystal Structure of A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha

All present enzymatic activity of Crystal Structure of A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha:
1.4.3.21;

Protein crystallography data

The structure of Crystal Structure of A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha, PDB code: 3loy was solved by V.J.Klema, 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) 37.42 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 288.510, 91.065, 151.098, 90.00, 117.23, 90.00
R / Rfree (%) 14.5 / 19.1

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha (pdb code 3loy). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Crystal Structure of A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha, PDB code: 3loy:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 3loy

Go back to Copper Binding Sites List in 3loy
Copper binding site 1 out of 3 in the Crystal Structure of A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha


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 A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu635

b:22.7
occ:1.00
ND1 A:HIS597 2.0 22.0 1.0
NE2 A:HIS436 2.0 22.5 1.0
NE2 A:HIS438 2.1 23.3 1.0
O A:HOH1582 2.6 36.5 1.0
O A:HOH772 2.6 23.8 1.0
CE1 A:HIS597 3.0 17.6 1.0
CG A:HIS597 3.0 22.1 1.0
CE1 A:HIS436 3.0 21.6 1.0
CD2 A:HIS436 3.0 17.8 1.0
CD2 A:HIS438 3.0 17.8 1.0
CE1 A:HIS438 3.1 17.0 1.0
CB A:HIS597 3.3 19.1 1.0
NE2 A:HIS597 4.1 21.2 1.0
ND1 A:HIS436 4.1 18.2 1.0
CD2 A:HIS597 4.1 20.4 1.0
CG A:HIS436 4.1 19.8 1.0
CG A:HIS438 4.2 20.2 1.0
ND1 A:HIS438 4.2 18.5 1.0
CE1 A:PHE595 4.3 28.9 1.0
O A:HOH695 4.4 18.6 1.0
O2 A:TPQ386 4.4 29.5 1.0
CZ A:PHE595 4.8 25.4 1.0
O A:HOH644 4.9 30.0 1.0
CA A:HIS597 4.9 19.4 1.0
O A:HOH1387 5.0 40.5 1.0

Copper binding site 2 out of 3 in 3loy

Go back to Copper Binding Sites List in 3loy
Copper binding site 2 out of 3 in the Crystal Structure of A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha


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 A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu635

b:24.9
occ:1.00
NE2 B:HIS436 1.9 18.3 1.0
ND1 B:HIS597 2.1 20.2 1.0
NE2 B:HIS438 2.1 20.9 1.0
O B:HOH831 2.3 26.1 1.0
O B:HOH1321 2.5 52.4 1.0
CE1 B:HIS436 2.8 20.5 1.0
CD2 B:HIS436 2.9 21.6 1.0
CD2 B:HIS438 3.0 18.1 1.0
CG B:HIS597 3.0 23.5 1.0
CE1 B:HIS597 3.2 18.9 1.0
CE1 B:HIS438 3.2 24.2 1.0
CB B:HIS597 3.3 19.1 1.0
ND1 B:HIS436 3.9 23.5 1.0
CG B:HIS436 4.0 21.5 1.0
CG B:HIS438 4.2 22.3 1.0
CD2 B:HIS597 4.2 19.6 1.0
NE2 B:HIS597 4.2 22.6 1.0
ND1 B:HIS438 4.3 24.3 1.0
O B:HOH718 4.3 18.1 1.0
CE1 B:PHE595 4.4 27.1 1.0
O2 B:TPQ386 4.7 25.6 1.0
O B:HOH1330 4.8 44.9 1.0
O B:HOH1546 4.8 34.1 1.0
CA B:HIS597 4.8 21.5 1.0
CZ B:PHE595 4.8 23.6 1.0

Copper binding site 3 out of 3 in 3loy

Go back to Copper Binding Sites List in 3loy
Copper binding site 3 out of 3 in the Crystal Structure of A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha


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 A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu635

b:21.2
occ:1.00
NE2 C:HIS438 2.0 19.9 1.0
NE2 C:HIS436 2.0 15.7 1.0
ND1 C:HIS597 2.0 17.9 1.0
O C:HOH884 2.4 39.9 1.0
O C:HOH653 2.5 22.0 1.0
CE1 C:HIS436 3.0 15.1 1.0
CE1 C:HIS438 3.0 21.9 1.0
CE1 C:HIS597 3.0 14.9 1.0
CD2 C:HIS438 3.0 18.2 1.0
CD2 C:HIS436 3.0 17.5 1.0
CG C:HIS597 3.0 20.2 1.0
CB C:HIS597 3.3 19.1 1.0
ND1 C:HIS436 4.1 15.6 1.0
ND1 C:HIS438 4.1 17.9 1.0
NE2 C:HIS597 4.1 16.7 1.0
CG C:HIS436 4.1 17.2 1.0
CG C:HIS438 4.1 19.8 1.0
CD2 C:HIS597 4.2 16.3 1.0
CE1 C:PHE595 4.3 23.6 1.0
O C:HOH861 4.4 19.3 1.0
O2 C:TPQ386 4.5 22.5 1.0
CZ C:PHE595 4.7 22.1 1.0
O C:HOH1687 4.8 46.0 1.0
CA C:HIS597 4.8 18.4 1.0
O C:HOH889 4.9 27.4 1.0
CD2 C:LEU410 4.9 15.0 1.0

Reference:

C.M.Chang, V.J.Klema, B.J.Johnson, M.Mure, J.P.Klinman, C.M.Wilmot. Kinetic and Structural Analysis of Substrate Specificity in Two Copper Amine Oxidases From Hansenula Polymorpha. Biochemistry V. 49 2540 2010.
ISSN: ISSN 0006-2960
PubMed: 20155950
DOI: 10.1021/BI901933D
Page generated: Wed Oct 28 14:24:33 2020
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