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Calcium in PDB 1oac: Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution

Enzymatic activity of Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution

All present enzymatic activity of Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution:
1.4.3.6;

Protein crystallography data

The structure of Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution, PDB code: 1oac was solved by M.R.Parsons, M.A.Convery, C.M.Wilmot, S.E.V.Phillips, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 135.732, 167.775, 81.904, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1oac:

The structure of Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution also contains other interesting chemical elements:

Copper (Cu) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution (pdb code 1oac). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution, PDB code: 1oac:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in 1oac

Go back to Calcium Binding Sites List in 1oac
Calcium binding site 1 out of 4 in the Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca802

b:16.5
occ:1.00
 OD1 A:ASP678 2.3 17.8 1.0
OD1 A:ASP535 2.3 15.4 1.0
OD1 A:ASP533 2.3 17.0 1.0
O A:LEU534 2.3 16.7 1.0
O A:ALA679 2.3 15.8 1.0
O A:HOH963 2.5 13.0 1.0
C A:LEU534 3.4 13.6 1.0
C A:ALA679 3.4 14.2 1.0
CG A:ASP678 3.5 24.6 1.0
CG A:ASP535 3.5 16.9 1.0
CG A:ASP533 3.6 18.4 1.0
N A:ALA679 3.6 16.6 1.0
NZ A:LYS133 3.6 16.2 1.0
N A:ASP535 4.1 12.0 1.0
CA A:ASP535 4.1 14.4 1.0
CA A:ALA679 4.1 15.6 1.0
N A:LEU534 4.1 14.5 1.0
C A:ASP533 4.1 14.4 1.0
OD2 A:ASP678 4.2 21.2 1.0
OD2 A:ASP533 4.2 16.0 1.0
C A:ASP678 4.2 16.8 1.0
CA A:ASP678 4.4 19.1 1.0
O A:ASP533 4.4 14.2 1.0
CB A:ASP535 4.4 11.5 1.0
OD2 A:ASP535 4.4 19.9 1.0
CA A:LEU534 4.4 12.7 1.0
O A:GLU539 4.5 19.6 1.0
CA A:ASP533 4.5 12.3 1.0
N A:VAL680 4.6 14.1 1.0
CB A:ASP678 4.6 18.6 1.0
CB A:ASP533 4.6 12.4 1.0
ND2 A:ASN541 4.8 9.2 1.0
CE A:LYS133 4.9 17.7 1.0
CB A:ALA679 4.9 14.8 1.0
CA A:VAL680 5.0 16.1 1.0

Calcium binding site 2 out of 4 in 1oac

Go back to Calcium Binding Sites List in 1oac
Calcium binding site 2 out of 4 in the Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca803

b:20.1
occ:1.00
 OE1 A:GLU672 2.3 20.6 1.0
O A:TYR667 2.3 18.6 1.0
O A:HOH997 2.4 19.1 1.0
OD1 A:ASP670 2.4 21.1 1.0
O A:HOH992 2.5 18.1 1.0
OE1 A:GLU573 2.7 21.8 1.0
OE2 A:GLU573 2.8 21.0 1.0
CD A:GLU573 3.0 29.9 1.0
CG A:ASP670 3.2 31.6 1.0
OD2 A:ASP670 3.3 34.8 1.0
CD A:GLU672 3.4 26.8 1.0
C A:TYR667 3.6 16.9 1.0
CG A:GLU672 3.6 21.2 1.0
CE1 A:HIS644 4.2 22.9 1.0
O A:HOH1057 4.4 46.4 1.0
CB A:GLU672 4.4 22.2 1.0
OE2 A:GLU672 4.4 28.4 1.0
ND1 A:HIS644 4.4 28.5 1.0
CA A:TYR667 4.5 17.6 1.0
OE1 A:GLU647 4.5 22.6 1.0
N A:SER668 4.5 17.2 1.0
CA A:SER668 4.5 20.8 1.0
CG A:GLU573 4.6 20.1 1.0
OE2 A:GLU647 4.6 25.2 1.0
CB A:ASP670 4.7 25.6 1.0
N A:GLU672 4.7 21.9 1.0
N A:ARG642 4.7 17.5 1.0
O A:HOH1140 4.8 48.7 1.0
CB A:ARG642 4.8 25.9 1.0
O A:ARG642 5.0 20.1 1.0
CB A:TYR667 5.0 20.7 1.0

Calcium binding site 3 out of 4 in 1oac

Go back to Calcium Binding Sites List in 1oac
Calcium binding site 3 out of 4 in the Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca802

b:18.4
occ:1.00
 OD1 B:ASP533 2.3 17.5 1.0
OD1 B:ASP535 2.3 17.7 1.0
OD1 B:ASP678 2.3 18.5 1.0
O B:ALA679 2.3 19.1 1.0
O B:LEU534 2.3 18.6 1.0
O B:HOH972 2.5 15.2 1.0
C B:LEU534 3.4 18.7 1.0
CG B:ASP533 3.5 16.7 1.0
C B:ALA679 3.5 19.0 1.0
CG B:ASP678 3.6 18.8 1.0
CG B:ASP535 3.6 19.3 1.0
NZ B:LYS133 3.6 22.7 1.0
N B:ALA679 3.6 18.6 1.0
N B:ASP535 4.1 14.4 1.0
OD2 B:ASP533 4.1 19.0 1.0
C B:ASP533 4.1 14.3 1.0
CA B:ASP535 4.1 13.7 1.0
N B:LEU534 4.1 13.2 1.0
CA B:ALA679 4.1 17.0 1.0
C B:ASP678 4.2 19.0 1.0
OD2 B:ASP678 4.2 20.3 1.0
O B:ASP533 4.3 15.9 1.0
OD2 B:ASP535 4.4 17.8 1.0
O B:GLU539 4.4 22.2 1.0
CB B:ASP535 4.4 15.0 1.0
CA B:LEU534 4.4 15.5 1.0
CA B:ASP678 4.4 17.4 1.0
CA B:ASP533 4.5 15.8 1.0
CB B:ASP533 4.6 13.6 1.0
N B:VAL680 4.6 15.5 1.0
CB B:ASP678 4.6 14.8 1.0
ND2 B:ASN541 4.7 12.8 1.0
CE B:LYS133 4.9 23.4 1.0
CA B:VAL680 5.0 15.0 1.0

Calcium binding site 4 out of 4 in 1oac

Go back to Calcium Binding Sites List in 1oac
Calcium binding site 4 out of 4 in the Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 Angstroems Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca803

b:22.7
occ:1.00
 OE2 B:GLU672 2.3 23.5 1.0
O B:HOH1005 2.4 21.2 1.0
O B:TYR667 2.4 21.3 1.0
OD1 B:ASP670 2.4 25.5 1.0
O B:HOH1000 2.5 20.8 1.0
OE2 B:GLU573 2.7 21.9 1.0
OE1 B:GLU573 2.7 24.6 1.0
CD B:GLU573 3.0 31.0 1.0
CG B:ASP670 3.3 40.0 1.0
CD B:GLU672 3.3 26.4 1.0
CG B:GLU672 3.4 23.8 1.0
OD2 B:ASP670 3.5 42.5 1.0
C B:TYR667 3.6 22.0 1.0
CD2 B:HIS644 4.3 24.3 1.0
NE2 B:HIS644 4.3 26.8 1.0
OE1 B:GLU647 4.4 23.8 1.0
O B:HOH1065 4.4 47.7 1.0
OE1 B:GLU672 4.4 34.4 1.0
CA B:TYR667 4.4 24.0 1.0
CG B:GLU573 4.5 23.1 1.0
CB B:GLU672 4.5 25.6 1.0
N B:SER668 4.5 19.0 1.0
CA B:SER668 4.6 22.8 1.0
OE2 B:GLU647 4.6 28.7 1.0
N B:GLU672 4.7 25.4 1.0
CB B:ASP670 4.7 34.0 1.0
N B:ARG642 4.8 25.1 1.0
O B:HOH1150 4.8 70.7 1.0
N B:ASN671 4.8 30.0 1.0
N B:ASP670 4.9 31.6 1.0
CB B:ARG642 4.9 29.0 1.0
CD B:GLU647 5.0 32.1 1.0
CB B:TYR667 5.0 25.5 1.0

Reference:

M.R.Parsons, M.A.Convery, C.M.Wilmot, K.D.Yadav, V.Blakeley, A.S.Corner, S.E.Phillips, M.J.Mcpherson, P.F.Knowles. Crystal Structure of A Quinoenzyme: Copper Amine Oxidase of Escherichia Coli at 2 A Resolution. Structure V. 3 1171 1995.
ISSN: ISSN 0969-2126
PubMed: 8591028
DOI: 10.1016/S0969-2126(01)00253-2
Page generated: Thu Jul 11 13:17:41 2024

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