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Copper in PDB 4ev2: Crystal Structure of Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine

Enzymatic activity of Crystal Structure of Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine

All present enzymatic activity of Crystal Structure of Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine:
1.4.3.21;

Protein crystallography data

The structure of Crystal Structure of Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine, PDB code: 4ev2 was solved by V.J.Klema, C.J.Solheid, C.M.Wilmot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.97 / 2.18
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 104.408, 232.834, 105.119, 90.00, 96.66, 90.00
R / Rfree (%) 15 / 20.1

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine (pdb code 4ev2). 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 Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine, PDB code: 4ev2:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 4ev2

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Copper binding site 1 out of 6 in the Crystal Structure of Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine


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 Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu702

b:21.9
occ:1.00
 NE2 A:HIS458 1.9 19.4 1.0
ND1 A:HIS624 2.0 18.2 1.0
NE2 A:HIS456 2.0 20.1 1.0
O2 A:PEO707 2.5 18.4 1.0
CD2 A:HIS458 2.9 21.2 1.0
CE1 A:HIS456 2.9 21.4 1.0
CE1 A:HIS624 2.9 22.4 1.0
CG A:HIS624 3.0 22.1 1.0
CE1 A:HIS458 3.0 24.7 1.0
CD2 A:HIS456 3.0 20.4 1.0
O1 A:PEO707 3.1 29.1 1.0
CB A:HIS624 3.3 21.3 1.0
ND1 A:HIS456 4.0 18.4 1.0
CG A:HIS458 4.1 19.4 1.0
NE2 A:HIS624 4.1 20.0 1.0
ND1 A:HIS458 4.1 21.4 1.0
CD2 A:HIS624 4.1 17.2 1.0
CG A:HIS456 4.1 22.1 1.0
O A:HOH1253 4.1 52.2 1.0
CE A:MET634 4.2 43.4 0.5
O A:HOH1365 4.5 24.0 1.0
OZ A:TYQ405 4.7 34.6 1.0
CD1 A:LEU425 4.8 35.0 1.0
CD1 A:ILE622 4.8 24.5 1.0
CA A:HIS624 4.8 20.0 1.0
CE A:MET634 5.0 28.0 0.5

Copper binding site 2 out of 6 in 4ev2

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Copper binding site 2 out of 6 in the Crystal Structure of Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine


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 Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu702

b:19.8
occ:1.00
 ND1 B:HIS624 2.0 17.7 1.0
NE2 B:HIS456 2.1 18.0 1.0
NE2 B:HIS458 2.1 18.1 1.0
O1 B:PEO708 2.3 22.0 1.0
O2 B:PEO708 2.8 16.4 1.0
CD2 B:HIS458 2.9 13.7 1.0
CD2 B:HIS456 2.9 18.6 1.0
CE1 B:HIS624 3.0 21.2 1.0
CG B:HIS624 3.0 21.0 1.0
CE1 B:HIS456 3.1 24.2 1.0
CE1 B:HIS458 3.2 13.6 1.0
CB B:HIS624 3.4 18.6 1.0
NE2 B:HIS624 4.1 23.8 1.0
CG B:HIS458 4.1 18.3 1.0
CG B:HIS456 4.1 19.2 1.0
CD2 B:HIS624 4.1 16.4 1.0
ND1 B:HIS456 4.1 16.6 1.0
O B:HOH1310 4.2 51.6 1.0
ND1 B:HIS458 4.2 14.9 1.0
O B:HOH839 4.5 15.0 1.0
OZ B:TYQ405 4.5 27.8 1.0
CD1 B:LEU425 4.7 38.1 1.0
O B:HOH1309 4.8 45.7 1.0
SD B:MET634 4.8 35.7 0.5
CD1 B:ILE622 4.9 28.5 1.0
CA B:HIS624 4.9 18.8 1.0
CE B:MET634 4.9 18.1 0.5

Copper binding site 3 out of 6 in 4ev2

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Copper binding site 3 out of 6 in the Crystal Structure of Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine


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 Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu701

b:25.2
occ:1.00
 NE2 C:HIS456 1.9 19.3 1.0
ND1 C:HIS624 2.0 21.7 1.0
NE2 C:HIS458 2.1 23.4 1.0
O C:HOH1225 2.5 64.9 1.0
O C:HOH1332 2.6 11.9 1.0
CD2 C:HIS456 2.8 17.1 1.0
CE1 C:HIS456 3.0 21.6 1.0
CD2 C:HIS458 3.0 19.9 1.0
CG C:HIS624 3.0 24.8 1.0
CE1 C:HIS624 3.1 22.0 1.0
CE1 C:HIS458 3.1 21.2 1.0
CB C:HIS624 3.3 22.8 1.0
CG C:HIS456 4.0 21.2 1.0
ND1 C:HIS456 4.0 16.7 1.0
CD2 C:HIS624 4.1 24.1 1.0
NE2 C:HIS624 4.2 22.8 1.0
CG C:HIS458 4.2 20.6 1.0
ND1 C:HIS458 4.2 21.8 1.0
O C:HOH837 4.5 22.8 1.0
OZ C:TYQ405 4.7 38.8 1.0
CD2 C:LEU425 4.7 36.4 1.0
CE C:MET634 4.8 26.0 0.5
CA C:HIS624 4.8 23.9 1.0
O C:HOH1321 4.9 45.3 1.0
CD1 C:ILE622 5.0 30.0 1.0

Copper binding site 4 out of 6 in 4ev2

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Copper binding site 4 out of 6 in the Crystal Structure of Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine


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 Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cu701

b:29.1
occ:1.00
 NE2 D:HIS458 2.0 29.9 1.0
NE2 D:HIS456 2.0 23.9 1.0
ND1 D:HIS624 2.1 24.9 1.0
O D:HOH1291 2.6 19.5 1.0
CD2 D:HIS456 2.9 26.7 1.0
CD2 D:HIS458 2.9 29.6 1.0
CE1 D:HIS458 3.0 32.7 1.0
CE1 D:HIS456 3.0 29.4 1.0
CG D:HIS624 3.0 27.6 1.0
CE1 D:HIS624 3.1 27.2 1.0
CB D:HIS624 3.3 25.9 1.0
CG D:HIS456 4.0 29.8 1.0
ND1 D:HIS456 4.1 26.2 1.0
ND1 D:HIS458 4.1 25.8 1.0
CG D:HIS458 4.1 28.4 1.0
CD2 D:HIS624 4.2 25.4 1.0
NE2 D:HIS624 4.2 28.5 1.0
O D:HOH1201 4.4 33.4 1.0
OZ D:TYQ405 4.5 39.0 1.0
CD1 D:LEU425 4.7 43.4 1.0
CA D:HIS624 4.8 27.1 1.0
SD D:MET634 4.9 53.5 1.0

Copper binding site 5 out of 6 in 4ev2

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Copper binding site 5 out of 6 in the Crystal Structure of Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine


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 Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cu701

b:19.9
occ:1.00
 ND1 E:HIS624 2.1 15.2 1.0
NE2 E:HIS456 2.1 14.6 1.0
NE2 E:HIS458 2.1 16.2 1.0
O1 E:PEO706 2.5 14.6 1.0
O2 E:PEO706 3.0 27.2 1.0
CD2 E:HIS456 3.0 20.2 1.0
CE1 E:HIS624 3.0 17.3 1.0
O E:HOH1127 3.0 69.0 1.0
CG E:HIS624 3.1 17.3 1.0
CE1 E:HIS458 3.1 17.9 1.0
CE1 E:HIS456 3.1 17.3 1.0
CD2 E:HIS458 3.1 18.0 1.0
CB E:HIS624 3.4 17.1 1.0
NE2 E:HIS624 4.2 18.2 1.0
ND1 E:HIS456 4.2 15.3 1.0
CG E:HIS456 4.2 14.3 1.0
CD2 E:HIS624 4.2 18.7 1.0
ND1 E:HIS458 4.2 16.5 1.0
CG E:HIS458 4.3 18.2 1.0
O E:HOH1045 4.4 15.5 1.0
CE E:MET634 4.6 28.8 0.4
OZ E:TYQ405 4.6 24.6 1.0
O E:HOH1144 4.7 59.8 1.0
CD1 E:LEU425 4.8 34.6 1.0
CE E:MET634 4.8 30.2 0.6
CA E:HIS624 4.9 16.9 1.0
CD1 E:ILE622 5.0 25.8 1.0
SD E:MET634 5.0 37.8 0.6

Copper binding site 6 out of 6 in 4ev2

Go back to Copper Binding Sites List in 4ev2
Copper binding site 6 out of 6 in the Crystal Structure of Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine


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 Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cu701

b:23.6
occ:1.00
 ND1 F:HIS624 1.9 15.4 1.0
NE2 F:HIS458 2.0 25.8 1.0
NE2 F:HIS456 2.1 23.6 1.0
O1 F:PEO707 2.2 18.4 1.0
CE1 F:HIS624 2.8 21.2 1.0
CD2 F:HIS458 2.8 24.1 1.0
CD2 F:HIS456 2.9 20.1 1.0
CG F:HIS624 3.0 23.9 1.0
CE1 F:HIS458 3.1 27.8 1.0
CE1 F:HIS456 3.1 23.9 1.0
O2 F:PEO707 3.4 29.6 1.0
CB F:HIS624 3.4 21.2 1.0
NE2 F:HIS624 4.0 18.1 1.0
CG F:HIS458 4.0 22.6 1.0
CD2 F:HIS624 4.1 21.4 1.0
CG F:HIS456 4.1 22.4 1.0
ND1 F:HIS458 4.1 25.3 1.0
ND1 F:HIS456 4.2 20.0 1.0
OZ F:TYQ405 4.5 35.6 1.0
O F:HOH1125 4.5 24.8 1.0
CD1 F:LEU425 4.6 36.6 1.0
CA F:HIS624 4.9 22.6 1.0

Reference:

V.J.Klema, C.J.Solheid, J.P.Klinman, C.M.Wilmot. Crystal Structure of Copper Amine Oxidase-1 From Hansenula Polymorpha in Complex with Ethylamine To Be Published.
Page generated: Wed Jul 31 02:50:16 2024

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