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Copper in PDB 2c10: The Structure of A Truncated, Soluble Version of Semicarbazide- Sensitive Amine Oxidase

Enzymatic activity of The Structure of A Truncated, Soluble Version of Semicarbazide- Sensitive Amine Oxidase

All present enzymatic activity of The Structure of A Truncated, Soluble Version of Semicarbazide- Sensitive Amine Oxidase:
1.4.3.6;

Protein crystallography data

The structure of The Structure of A Truncated, Soluble Version of Semicarbazide- Sensitive Amine Oxidase, PDB code: 2c10 was solved by E.Jakobsson, G.J.Kleywegt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.50
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 130.236, 130.236, 221.529, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 25.2

Other elements in 2c10:

The structure of The Structure of A Truncated, Soluble Version of Semicarbazide- Sensitive Amine Oxidase also contains other interesting chemical elements:

Chlorine (Cl) 8 atoms
Calcium (Ca) 8 atoms

Copper Binding Sites:

The binding sites of Copper atom in the The Structure of A Truncated, Soluble Version of Semicarbazide- Sensitive Amine Oxidase (pdb code 2c10). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the The Structure of A Truncated, Soluble Version of Semicarbazide- Sensitive Amine Oxidase, PDB code: 2c10:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 2c10

Go back to Copper Binding Sites List in 2c10
Copper binding site 1 out of 4 in the The Structure of A Truncated, Soluble Version of Semicarbazide- Sensitive Amine Oxidase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of The Structure of A Truncated, Soluble Version of Semicarbazide- Sensitive Amine Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1772

b:33.4
occ:1.00
 NE2 A:HIS522 2.0 33.7 1.0
ND1 A:HIS684 2.0 29.9 1.0
NE2 A:HIS520 2.2 29.3 1.0
O A:HOH2089 2.4 28.6 1.0
CE1 A:HIS684 3.0 29.6 1.0
CD2 A:HIS522 3.0 32.5 1.0
CE1 A:HIS522 3.0 34.6 1.0
CE1 A:HIS520 3.1 28.4 1.0
CG A:HIS684 3.1 28.8 1.0
CD2 A:HIS520 3.2 28.2 1.0
CB A:HIS684 3.5 27.9 1.0
NE2 A:HIS684 4.1 29.8 1.0
ND1 A:HIS522 4.1 34.1 1.0
CG A:HIS522 4.2 32.8 1.0
CD2 A:HIS684 4.2 28.2 1.0
ND1 A:HIS520 4.2 27.3 1.0
O2 A:TPQ471 4.3 52.8 1.0
CG A:HIS520 4.3 28.4 1.0
O A:HOH2073 4.5 35.5 1.0
CE1 A:PHE682 4.8 29.3 1.0
OG1 A:THR694 4.9 35.1 1.0
CA A:HIS684 5.0 28.0 1.0

Copper binding site 2 out of 4 in 2c10

Go back to Copper Binding Sites List in 2c10
Copper binding site 2 out of 4 in the The Structure of A Truncated, Soluble Version of Semicarbazide- Sensitive Amine Oxidase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of The Structure of A Truncated, Soluble Version of Semicarbazide- Sensitive Amine Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1776

b:35.2
occ:1.00
 ND1 B:HIS684 2.0 31.9 1.0
NE2 B:HIS522 2.1 34.8 1.0
NE2 B:HIS520 2.2 31.4 1.0
O B:HOH2079 2.7 14.4 1.0
CE1 B:HIS684 2.9 30.6 1.0
CD2 B:HIS522 2.9 33.3 1.0
CE1 B:HIS520 3.1 31.4 1.0
CG B:HIS684 3.1 29.3 1.0
CE1 B:HIS522 3.2 34.9 1.0
CD2 B:HIS520 3.2 29.8 1.0
CB B:HIS684 3.5 28.8 1.0
NE2 B:HIS684 4.1 29.6 1.0
CG B:HIS522 4.2 32.2 1.0
O2 B:TPQ471 4.2 49.2 1.0
CD2 B:HIS684 4.2 30.0 1.0
ND1 B:HIS522 4.2 34.4 1.0
ND1 B:HIS520 4.2 29.7 1.0
CG B:HIS520 4.3 29.5 1.0
O B:HOH2054 4.4 31.1 1.0
OG1 B:THR694 4.9 35.9 1.0

Copper binding site 3 out of 4 in 2c10

Go back to Copper Binding Sites List in 2c10
Copper binding site 3 out of 4 in the The Structure of A Truncated, Soluble Version of Semicarbazide- Sensitive Amine Oxidase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of The Structure of A Truncated, Soluble Version of Semicarbazide- Sensitive Amine Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu1772

b:36.5
occ:1.00
 NE2 C:HIS522 2.1 34.3 1.0
NE2 C:HIS520 2.1 26.6 1.0
ND1 C:HIS684 2.1 26.9 1.0
O C:HOH2078 2.7 28.1 1.0
CE1 C:HIS520 3.0 26.3 1.0
CD2 C:HIS522 3.0 33.0 1.0
CE1 C:HIS684 3.1 27.1 1.0
CE1 C:HIS522 3.1 35.5 1.0
CG C:HIS684 3.1 25.9 1.0
CD2 C:HIS520 3.2 26.5 1.0
CB C:HIS684 3.5 25.8 1.0
ND1 C:HIS520 4.1 27.8 1.0
NE2 C:HIS684 4.2 26.0 1.0
ND1 C:HIS522 4.2 35.9 1.0
CG C:HIS522 4.2 32.8 1.0
CD2 C:HIS684 4.2 25.3 1.0
CG C:HIS520 4.3 28.1 1.0
O C:HOH2065 4.4 38.6 1.0
O2 C:TPQ471 4.4 49.9 1.0
CE1 C:PHE682 4.9 28.6 1.0
OG1 C:THR694 4.9 35.8 1.0
CB C:ALA491 4.9 36.8 1.0
CA C:HIS684 5.0 26.3 1.0

Copper binding site 4 out of 4 in 2c10

Go back to Copper Binding Sites List in 2c10
Copper binding site 4 out of 4 in the The Structure of A Truncated, Soluble Version of Semicarbazide- Sensitive Amine Oxidase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of The Structure of A Truncated, Soluble Version of Semicarbazide- Sensitive Amine Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cu1777

b:35.3
occ:1.00
 NE2 D:HIS522 2.1 38.5 1.0
ND1 D:HIS684 2.1 31.6 1.0
NE2 D:HIS520 2.2 32.6 1.0
O D:HOH2068 2.4 12.2 1.0
CE1 D:HIS684 3.0 29.9 1.0
CD2 D:HIS522 3.0 36.5 1.0
CE1 D:HIS522 3.1 38.3 1.0
CG D:HIS684 3.1 29.5 1.0
CE1 D:HIS520 3.1 34.2 1.0
CD2 D:HIS520 3.2 32.9 1.0
CB D:HIS684 3.5 28.6 1.0
NE2 D:HIS684 4.1 30.9 1.0
O2 D:TPQ471 4.2 49.7 1.0
ND1 D:HIS522 4.2 37.2 1.0
CG D:HIS522 4.2 35.7 1.0
CD2 D:HIS684 4.2 30.4 1.0
ND1 D:HIS520 4.3 33.8 1.0
O D:HOH2049 4.3 31.6 1.0
CG D:HIS520 4.4 33.1 1.0

Reference:

E.Jakobsson, J.Nilsson, D.Ogg, G.J.Kleywegt. Structure of Human Semicarbazide-Sensitive Amine Oxidase/Vascular Adhesion Protein-1. Acta Crystallogr. D Biol. V. 61 1550 2005CRYSTALLOGR..
ISSN: ISSN 0907-4449
PubMed: 16239734
DOI: 10.1107/S0907444905028805
Page generated: Tue Jul 30 23:17:06 2024

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