Copper in PDB 2c11: Crystal Structure of the 2-Hydrazinopyridine of Semicarbazide- Sensitive Amine Oxidase

All present enzymatic activity of Crystal Structure of the 2-Hydrazinopyridine of Semicarbazide- Sensitive Amine Oxidase:
1.4.3.6;

The structure of Crystal Structure of the 2-Hydrazinopyridine of Semicarbazide- Sensitive Amine Oxidase, PDB code: 2c11 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 / 2.90
Space group	P 43
Cell size a, b, c (Å), α, β, γ (°)	127.402, 127.402, 219.361, 90.00, 90.00, 90.00
R / Rfree (%)	21.5 / 27.6

The structure of Crystal Structure of the 2-Hydrazinopyridine of Semicarbazide- Sensitive Amine Oxidase also contains other interesting chemical elements:

Chlorine	(Cl)	4 atoms
Calcium	(Ca)	8 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30;

Binding sites:

The binding sites of Copper atom in the Crystal Structure of the 2-Hydrazinopyridine of Semicarbazide- Sensitive Amine Oxidase (pdb code 2c11). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 30 binding sites of Copper where determined in the Crystal Structure of the 2-Hydrazinopyridine of Semicarbazide- Sensitive Amine Oxidase, PDB code: 2c11:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Copper binding site 1 out of 30 in the Crystal Structure of the 2-Hydrazinopyridine 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 Crystal Structure of the 2-Hydrazinopyridine of Semicarbazide- Sensitive Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1737 b:49.8 occ:1.00 NE2 A:HIS522 2.0 49.0 1.0 ND1 A:HIS684 2.0 45.6 1.0 NE2 A:HIS520 2.2 47.9 1.0 O A:HOH2018 2.6 35.8 1.0 CD2 A:HIS522 2.8 49.2 1.0 CE1 A:HIS684 3.0 44.5 1.0 CG A:HIS684 3.0 46.4 1.0 CE1 A:HIS520 3.1 48.4 1.0 CE1 A:HIS522 3.2 49.2 1.0 CD2 A:HIS520 3.2 48.4 1.0 CB A:HIS684 3.4 46.1 1.0 O2 A:PAQ471 3.7 63.0 1.0 CG A:HIS522 4.0 48.7 1.0 NE2 A:HIS684 4.1 44.9 1.0 ND1 A:HIS522 4.1 49.4 1.0 CD2 A:HIS684 4.2 45.7 1.0 ND1 A:HIS520 4.2 49.0 1.0 CG A:HIS520 4.4 46.9 1.0 CD1 A:PAQ471 4.8 60.4 1.0 CA A:HIS684 4.9 44.5 1.0 CG2 A:ILE495 5.0 59.7 1.0 CB A:ALA491 5.0 58.7 1.0

Copper binding site 2 out of 30 in the Crystal Structure of the 2-Hydrazinopyridine 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 Crystal Structure of the 2-Hydrazinopyridine of Semicarbazide- Sensitive Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1740 b:81.5 occ:1.00 NE2 A:HIS112 2.3 80.0 1.0 CE1 A:HIS112 3.3 79.6 1.0 CD2 A:HIS112 3.3 78.7 1.0 O A:HOH2001 4.1 41.5 1.0 ND1 A:HIS112 4.4 79.1 1.0 CG A:HIS112 4.4 79.1 1.0

Copper binding site 3 out of 30 in the Crystal Structure of the 2-Hydrazinopyridine 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 Crystal Structure of the 2-Hydrazinopyridine of Semicarbazide- Sensitive Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1741 b:83.2 occ:1.00 NE2 A:HIS160 2.3 77.2 1.0 OE2 A:GLU140 2.7 73.4 1.0 CE1 A:HIS160 2.9 78.5 1.0 CD A:GLU140 3.2 73.5 1.0 OE1 A:GLU140 3.3 72.1 1.0 O A:HOH2015 3.3 32.2 1.0 OG A:SER646 3.6 57.0 1.0 CD2 A:HIS160 3.6 77.5 1.0 ND1 A:HIS160 4.2 78.5 1.0 CE1 A:PHE648 4.2 60.7 1.0 CD A:ARG159 4.4 77.5 1.0 CD1 A:PHE648 4.4 60.5 1.0 CG A:GLU140 4.5 73.6 1.0 CG A:HIS160 4.5 78.6 1.0 CB A:SER646 4.6 60.2 1.0 CG A:ARG159 4.9 77.8 1.0

Copper binding site 4 out of 30 in the Crystal Structure of the 2-Hydrazinopyridine 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 Crystal Structure of the 2-Hydrazinopyridine of Semicarbazide- Sensitive Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1742 b:77.3 occ:1.00 ND1 A:HIS167 2.6 77.2 1.0 CG A:HIS167 3.2 77.7 1.0 CE1 A:HIS167 3.2 79.2 1.0 CB A:HIS167 3.6 75.7 1.0 CD2 A:HIS167 4.0 78.9 1.0 NE2 A:HIS167 4.0 80.4 1.0 N A:HIS167 4.0 74.6 1.0 CB A:PRO165 4.0 73.9 1.0 CA A:HIS167 4.4 74.8 1.0 CA A:GLY221 4.6 64.8 1.0 N A:TYR166 4.6 73.8 1.0 O A:GLY221 4.7 64.5 1.0 CA A:PRO165 4.7 74.4 1.0 C A:PRO165 4.8 73.8 1.0 NZ A:LYS252 4.8 62.3 1.0

Copper binding site 5 out of 30 in the Crystal Structure of the 2-Hydrazinopyridine 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 5 of Crystal Structure of the 2-Hydrazinopyridine of Semicarbazide- Sensitive Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1743 b:84.4 occ:1.00 NE2 A:HIS414 2.4 73.7 1.0 CE1 A:HIS414 2.6 72.3 1.0 CD2 A:HIS414 3.6 72.5 1.0 CB A:ASP412 3.7 65.4 1.0 ND1 A:HIS414 3.8 71.2 1.0 CG A:HIS414 4.3 72.1 1.0 NH2 A:ARG65 4.4 83.0 1.0 CG A:ASP412 4.5 67.7 1.0 OD2 A:ASP412 4.6 68.8 1.0 C A:ASP412 4.7 64.8 1.0 CA A:ASP412 4.7 64.9 1.0 CG2 A:THR424 4.8 67.5 1.0 O A:ASP412 4.9 65.5 1.0 N A:TRP413 4.9 65.2 1.0 N A:ASP412 5.0 64.8 1.0

Copper binding site 6 out of 30 in the Crystal Structure of the 2-Hydrazinopyridine 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 6 of Crystal Structure of the 2-Hydrazinopyridine of Semicarbazide- Sensitive Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1744 b:74.2 occ:1.00 OD1 A:ASP446 2.2 62.8 1.0 NE2 A:HIS444 2.5 60.1 1.0 CG A:ASP446 3.0 62.3 1.0 OD2 A:ASP446 3.1 60.9 1.0 CE1 A:HIS444 3.4 62.2 1.0 CD2 A:HIS444 3.4 60.1 1.0 O A:GLY727 3.9 74.8 1.0 ND1 A:HIS450 4.2 66.0 1.0 CG B:PRO397 4.3 53.6 1.0 O A:SER445 4.4 59.0 1.0 CB A:ASP446 4.4 61.2 1.0 ND1 A:HIS444 4.5 61.2 1.0 CG A:HIS444 4.5 60.6 1.0 CD B:PRO397 4.7 53.6 1.0 CA A:ASP446 4.8 59.7 1.0 C A:GLY727 4.8 75.2 1.0 C A:SER445 5.0 59.3 1.0

Copper binding site 7 out of 30 in the Crystal Structure of the 2-Hydrazinopyridine 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 7 of Crystal Structure of the 2-Hydrazinopyridine of Semicarbazide- Sensitive Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1745 b:80.8 occ:1.00 NE2 A:HIS687 2.3 47.9 1.0 CE1 A:HIS687 3.0 47.4 1.0 CD2 A:HIS687 3.4 47.6 1.0 OD1 A:ASP690 3.5 47.5 1.0 NH2 B:ARG706 3.8 55.2 1.0 NE2 A:HIS684 3.9 44.9 1.0 OD2 A:ASP690 4.0 45.5 1.0 CD2 A:HIS684 4.1 45.7 1.0 OH B:TYR586 4.1 53.6 1.0 CG A:ASP690 4.1 47.4 1.0 ND1 A:HIS687 4.2 47.7 1.0 ND2 A:ASN699 4.3 55.9 1.0 CG A:HIS687 4.4 47.2 1.0 CE1 A:HIS684 4.8 44.5 1.0 CG2 A:THR694 5.0 53.1 1.0 CZ B:ARG706 5.0 55.3 1.0

Copper binding site 8 out of 30 in the Crystal Structure of the 2-Hydrazinopyridine 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 8 of Crystal Structure of the 2-Hydrazinopyridine of Semicarbazide- Sensitive Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu1742 b:55.4 occ:1.00 ND1 B:HIS684 2.0 45.5 1.0 NE2 B:HIS522 2.0 49.5 1.0 NE2 B:HIS520 2.2 52.2 1.0 O B:HOH2019 2.4 10.7 1.0 CE1 B:HIS522 2.7 50.3 1.0 CE1 B:HIS684 2.8 47.2 1.0 CG B:HIS684 3.1 46.3 1.0 CE1 B:HIS520 3.2 53.0 1.0 CD2 B:HIS522 3.2 48.8 1.0 CD2 B:HIS520 3.2 50.8 1.0 CB B:HIS684 3.5 44.2 1.0 O2 B:PAQ471 3.7 60.8 1.0 ND1 B:HIS522 3.9 49.9 1.0 NE2 B:HIS684 4.0 44.5 1.0 CD2 B:HIS684 4.1 44.9 1.0 CG B:HIS522 4.2 50.1 1.0 ND1 B:HIS520 4.3 52.5 1.0 CG B:HIS520 4.4 51.2 1.0 CG2 B:ILE495 4.5 54.9 1.0 CD1 B:PAQ471 4.7 59.8 1.0

Copper binding site 9 out of 30 in the Crystal Structure of the 2-Hydrazinopyridine 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 9 of Crystal Structure of the 2-Hydrazinopyridine of Semicarbazide- Sensitive Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu1744 b:76.0 occ:1.00 NE2 B:HIS112 2.5 73.5 1.0 CE1 B:HIS112 2.7 72.8 1.0 CD2 B:HIS112 3.8 72.2 1.0 ND1 B:HIS112 4.0 71.7 1.0 CG B:HIS112 4.6 71.6 1.0

Copper binding site 10 out of 30 in the Crystal Structure of the 2-Hydrazinopyridine 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 10 of Crystal Structure of the 2-Hydrazinopyridine of Semicarbazide- Sensitive Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu1745 b:75.3 occ:1.00 OE1 B:GLU140 2.2 74.0 1.0 NE2 B:HIS160 2.4 69.3 1.0 CE1 B:HIS160 2.4 70.0 1.0 CD B:GLU140 3.1 74.0 1.0 OE2 B:GLU140 3.2 73.4 1.0 CD2 B:HIS160 3.6 69.9 1.0 ND1 B:HIS160 3.6 70.3 1.0 CE1 B:PHE648 3.7 59.1 1.0 OG B:SER646 3.8 59.0 1.0 CD1 B:PHE648 4.1 58.6 1.0 CG B:HIS160 4.2 70.6 1.0 CG2 B:THR657 4.4 60.8 1.0 CG B:GLU140 4.5 73.7 1.0 CZ B:PHE648 4.8 58.0 1.0 CB B:SER646 4.9 59.8 1.0

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