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Calcium in PDB 2woh: Strontium Soaked E. Coli Copper Amine Oxidase

Enzymatic activity of Strontium Soaked E. Coli Copper Amine Oxidase

All present enzymatic activity of Strontium Soaked E. Coli Copper Amine Oxidase:
1.4.3.6;

Protein crystallography data

The structure of Strontium Soaked E. Coli Copper Amine Oxidase, PDB code: 2woh was solved by M.A.Smith, P.Pirrat, A.R.Pearson, P.F.Knowles, S.E.V.Phillips, M.J.Mcpherson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.82 / 2.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 135.135, 166.911, 79.796, 90.00, 90.00, 90.00
R / Rfree (%) 18.564 / 24.28

Other elements in 2woh:

The structure of Strontium Soaked E. Coli Copper Amine Oxidase also contains other interesting chemical elements:

Strontium (Sr) 2 atoms
Copper (Cu) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Strontium Soaked E. Coli Copper Amine Oxidase (pdb code 2woh). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Strontium Soaked E. Coli Copper Amine Oxidase, PDB code: 2woh:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 2woh

Go back to Calcium Binding Sites List in 2woh
Calcium binding site 1 out of 2 in the Strontium Soaked E. Coli Copper Amine Oxidase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Strontium Soaked E. Coli Copper Amine Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca802

b:34.5
occ:1.00
OD1 A:ASP535 2.2 33.7 1.0
O A:LEU534 2.2 33.8 1.0
O A:HOH2281 2.3 27.7 1.0
O A:ALA679 2.3 36.0 1.0
OD1 A:ASP533 2.3 33.1 1.0
OD1 A:ASP678 2.4 37.3 1.0
C A:LEU534 3.3 33.7 1.0
C A:ALA679 3.5 36.1 1.0
CG A:ASP535 3.5 33.7 1.0
CG A:ASP678 3.6 37.4 1.0
NZ A:LYS133 3.6 41.1 1.0
CG A:ASP533 3.6 33.2 1.0
N A:ALA679 3.6 36.7 1.0
C A:ASP533 4.0 33.5 1.0
N A:ASP535 4.0 33.8 1.0
CA A:ASP535 4.0 33.8 1.0
N A:LEU534 4.1 33.6 1.0
CA A:ALA679 4.1 36.4 1.0
O A:ASP533 4.2 33.5 1.0
C A:ASP678 4.2 37.1 1.0
OD2 A:ASP678 4.2 37.4 1.0
OD2 A:ASP535 4.3 32.9 1.0
CA A:LEU534 4.3 33.7 1.0
OD2 A:ASP533 4.3 33.4 1.0
CA A:ASP533 4.4 33.4 1.0
CB A:ASP535 4.4 33.7 1.0
CA A:ASP678 4.5 37.4 1.0
O A:GLU539 4.5 34.8 1.0
N A:VAL680 4.5 35.8 1.0
CB A:ASP533 4.6 33.4 1.0
CB A:ASP678 4.6 37.3 1.0
OD1 A:ASN541 4.8 33.3 1.0
CA A:VAL680 4.8 35.5 1.0
CG2 A:VAL680 4.8 35.4 1.0
CE A:LYS133 4.9 41.1 1.0
O A:ASP678 4.9 36.9 1.0

Calcium binding site 2 out of 2 in 2woh

Go back to Calcium Binding Sites List in 2woh
Calcium binding site 2 out of 2 in the Strontium Soaked E. Coli Copper Amine Oxidase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Strontium Soaked E. Coli Copper Amine Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca802

b:38.0
occ:1.00
O B:ALA679 2.2 38.8 1.0
OD1 B:ASP533 2.2 33.5 1.0
O B:LEU534 2.2 33.6 1.0
OD1 B:ASP535 2.3 32.5 1.0
OD1 B:ASP678 2.3 40.9 1.0
O B:HOH2203 2.4 27.4 1.0
C B:LEU534 3.3 33.5 1.0
C B:ALA679 3.3 38.9 1.0
NZ B:LYS133 3.4 46.7 1.0
N B:ALA679 3.5 40.0 1.0
CG B:ASP533 3.5 33.4 1.0
CG B:ASP535 3.5 33.3 1.0
CG B:ASP678 3.5 41.1 1.0
C B:ASP533 3.9 33.2 1.0
CA B:ALA679 3.9 39.4 1.0
N B:LEU534 4.0 33.3 1.0
N B:ASP535 4.1 33.5 1.0
O B:ASP533 4.1 33.1 1.0
OD2 B:ASP678 4.2 41.1 1.0
C B:ASP678 4.2 40.5 1.0
OD2 B:ASP533 4.2 33.8 1.0
CA B:ASP535 4.2 33.6 1.0
CA B:LEU534 4.3 33.4 1.0
OD2 B:ASP535 4.3 32.3 1.0
CA B:ASP533 4.3 33.1 1.0
N B:VAL680 4.4 38.5 1.0
CA B:ASP678 4.4 41.0 1.0
CB B:ASP535 4.5 33.6 1.0
CB B:ASP533 4.5 33.1 1.0
O B:GLU539 4.5 36.2 1.0
CB B:ASP678 4.6 41.0 1.0
CE B:LYS133 4.6 46.8 1.0
CA B:VAL680 4.7 38.2 1.0
CB B:ALA679 4.8 39.3 1.0
CG2 B:VAL680 4.9 38.1 1.0
OD1 B:ASN541 5.0 35.8 1.0

Reference:

M.A.Smith, P.Pirrat, A.R.Pearson, C.R.Kurtis, T.G.Gaule, P.F.Knowles, S.E.Phillips, M.J.Mcpherson. Exploring the Roles of the Metal Ions in Escherichia Coli Copper Amine Oxidase. Biochemistry V. 49 1268 2010.
ISSN: ISSN 0006-2960
PubMed: 20052994
DOI: 10.1021/BI901738K
Page generated: Fri Jul 12 18:47:24 2024

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