Atomistry » Calcium » PDB 2vuz-2w3i » 2w0q
Atomistry »
  Calcium »
    PDB 2vuz-2w3i »
      2w0q »

Calcium in PDB 2w0q: E. Coli Copper Amine Oxidase in Complex with Xenon

Enzymatic activity of E. Coli Copper Amine Oxidase in Complex with Xenon

All present enzymatic activity of E. Coli Copper Amine Oxidase in Complex with Xenon:
1.4.3.4;

Protein crystallography data

The structure of E. Coli Copper Amine Oxidase in Complex with Xenon, PDB code: 2w0q was solved by P.Pirrat, M.A.Smith, A.R.Pearson, M.J.Mcpherson, S.E.V.Phillips, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.27 / 2.48
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 134.588, 166.871, 80.330, 90.00, 90.00, 90.00
R / Rfree (%) 15.8 / 21.9

Other elements in 2w0q:

The structure of E. Coli Copper Amine Oxidase in Complex with Xenon also contains other interesting chemical elements:

Xenon (Xe) 11 atoms
Copper (Cu) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the E. Coli Copper Amine Oxidase in Complex with Xenon (pdb code 2w0q). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the E. Coli Copper Amine Oxidase in Complex with Xenon, PDB code: 2w0q:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in 2w0q

Go back to Calcium Binding Sites List in 2w0q
Calcium binding site 1 out of 4 in the E. Coli Copper Amine Oxidase in Complex with Xenon


Mono view


Stereo pair view

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

b:27.3
occ:1.00
OD1 A:ASP535 2.2 28.4 1.0
OD1 A:ASP533 2.3 24.3 1.0
OD1 A:ASP678 2.3 33.0 1.0
O A:HOH2254 2.3 27.0 1.0
O A:LEU534 2.3 29.4 1.0
O A:ALA679 2.4 28.8 1.0
C A:LEU534 3.4 29.4 1.0
C A:ALA679 3.5 30.3 1.0
CG A:ASP535 3.5 28.5 1.0
N A:ALA679 3.5 32.1 1.0
CG A:ASP678 3.5 35.7 1.0
CG A:ASP533 3.6 27.9 1.0
NZ A:LYS133 3.7 27.1 1.0
C A:ASP533 4.0 28.3 1.0
CA A:ALA679 4.1 30.9 1.0
CA A:ASP535 4.1 28.2 1.0
N A:ASP535 4.1 28.9 1.0
C A:ASP678 4.2 33.3 1.0
N A:LEU534 4.2 28.7 1.0
OD2 A:ASP678 4.2 38.5 1.0
O A:ASP533 4.3 29.9 1.0
OD2 A:ASP535 4.3 29.8 1.0
OD2 A:ASP533 4.3 29.0 1.0
CA A:ASP678 4.4 33.9 1.0
CA A:LEU534 4.4 29.2 1.0
CB A:ASP535 4.4 27.2 1.0
CA A:ASP533 4.4 27.7 1.0
O A:GLU539 4.5 32.3 1.0
N A:VAL680 4.6 29.8 1.0
CB A:ASP678 4.6 33.6 1.0
CB A:ASP533 4.6 26.9 1.0
ND2 A:ASN541 4.7 28.3 1.0
CB A:ALA679 4.9 29.8 1.0
CA A:VAL680 5.0 29.2 1.0
O A:ASP678 5.0 33.1 1.0

Calcium binding site 2 out of 4 in 2w0q

Go back to Calcium Binding Sites List in 2w0q
Calcium binding site 2 out of 4 in the E. Coli Copper Amine Oxidase in Complex with Xenon


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of E. Coli Copper Amine Oxidase in Complex with Xenon within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca803

b:69.8
occ:1.00
O A:HOH2290 2.2 40.9 1.0
O A:TYR667 2.5 41.9 1.0
O A:HOH2294 2.6 39.1 1.0
OE2 A:GLU573 2.6 36.1 1.0
OE1 A:GLU672 2.8 53.9 1.0
O A:HOH2268 3.2 55.6 1.0
OE1 A:GLU573 3.3 37.7 1.0
CD A:GLU573 3.3 38.7 1.0
O A:HOH2307 3.4 53.0 1.0
C A:TYR667 3.7 42.0 1.0
CD A:GLU672 3.9 52.8 1.0
OE1 A:GLU647 4.0 38.9 1.0
N A:ARG642 4.2 33.5 1.0
OE2 A:GLU647 4.4 38.5 1.0
CG A:GLU672 4.4 47.1 1.0
CA A:TYR667 4.4 41.7 1.0
O A:ARG642 4.5 32.9 1.0
CB A:THR641 4.5 32.7 1.0
CD A:GLU647 4.6 40.3 1.0
CB A:ARG642 4.6 33.9 1.0
N A:SER668 4.7 43.2 1.0
CB A:TYR667 4.7 42.0 1.0
CA A:SER668 4.8 44.1 1.0
CG A:GLU573 4.8 37.2 1.0
CG2 A:THR641 4.9 32.6 1.0
CA A:ARG642 4.9 34.3 1.0

Calcium binding site 3 out of 4 in 2w0q

Go back to Calcium Binding Sites List in 2w0q
Calcium binding site 3 out of 4 in the E. Coli Copper Amine Oxidase in Complex with Xenon


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of E. Coli Copper Amine Oxidase in Complex with Xenon within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca802

b:31.2
occ:1.00
OD1 B:ASP535 2.3 30.0 1.0
OD1 B:ASP533 2.3 26.5 1.0
OD1 B:ASP678 2.4 33.5 1.0
O B:HOH2204 2.4 25.5 1.0
O B:ALA679 2.4 34.6 1.0
O B:LEU534 2.4 32.7 1.0
C B:LEU534 3.4 31.4 1.0
CG B:ASP535 3.5 30.6 1.0
C B:ALA679 3.5 33.4 1.0
CG B:ASP678 3.6 33.4 1.0
CG B:ASP533 3.6 31.8 1.0
NZ B:LYS133 3.6 34.3 1.0
N B:ALA679 3.7 33.6 1.0
C B:ASP533 4.0 30.5 1.0
N B:ASP535 4.1 30.9 1.0
N B:LEU534 4.1 29.5 1.0
CA B:ASP535 4.1 30.2 1.0
O B:ASP533 4.1 31.3 1.0
OD2 B:ASP678 4.3 29.1 1.0
CA B:ALA679 4.3 33.0 1.0
C B:ASP678 4.3 33.7 1.0
OD2 B:ASP535 4.3 32.0 1.0
CA B:LEU534 4.3 30.9 1.0
OD2 B:ASP533 4.4 31.0 1.0
CA B:ASP533 4.4 30.3 1.0
CB B:ASP535 4.4 29.5 1.0
CA B:ASP678 4.5 32.9 1.0
N B:VAL680 4.5 32.7 1.0
CB B:ASP533 4.6 30.2 1.0
ND2 B:ASN541 4.6 31.8 1.0
O B:GLU539 4.6 38.2 1.0
CB B:ASP678 4.7 32.4 1.0
CG2 B:VAL680 4.7 31.9 1.0
CA B:VAL680 4.8 31.3 1.0
CE B:LYS133 4.9 35.1 1.0
CB B:ALA679 5.0 32.8 1.0

Calcium binding site 4 out of 4 in 2w0q

Go back to Calcium Binding Sites List in 2w0q
Calcium binding site 4 out of 4 in the E. Coli Copper Amine Oxidase in Complex with Xenon


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of E. Coli Copper Amine Oxidase in Complex with Xenon within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca803

b:77.6
occ:1.00
OE2 B:GLU573 2.4 33.9 1.0
O B:TYR667 2.4 48.0 1.0
OE2 B:GLU672 2.5 58.4 1.0
O B:HOH2232 2.9 56.9 1.0
CD B:GLU573 3.0 39.0 1.0
OE1 B:GLU573 3.1 40.4 1.0
CD B:GLU672 3.4 57.7 1.0
C B:TYR667 3.6 47.9 1.0
CG B:GLU672 3.8 53.2 1.0
N B:ARG642 4.2 37.4 1.0
OE1 B:GLU647 4.2 51.0 1.0
CB B:THR641 4.3 35.5 1.0
CA B:TYR667 4.4 47.3 1.0
CB B:ARG642 4.5 37.2 1.0
OE1 B:GLU672 4.5 62.0 1.0
CG B:GLU573 4.5 40.4 1.0
N B:SER668 4.5 48.7 1.0
CA B:SER668 4.6 49.7 1.0
OE2 B:GLU647 4.6 52.4 1.0
CB B:GLU672 4.6 50.2 1.0
O B:ARG642 4.7 36.5 1.0
CG2 B:THR641 4.7 36.4 1.0
CB B:TYR667 4.8 46.2 1.0
CA B:THR641 4.9 35.4 1.0
CD B:GLU647 4.9 51.5 1.0
CA B:ARG642 4.9 37.6 1.0
CG B:ARG642 4.9 38.0 1.0

Reference:

P.Pirrat, M.A.Smith, A.R.Pearson, M.J.Mcpherson, S.E.V.Phillips. Structure of A Xenon Derivative of Escherichia Coli Copper Amine Oxidase: Confirmation of the Proposed Oxygen-Entry Pathway. Acta Crystallogr.,Sect.F V. 64 1105 2008.
ISSN: ISSN 1744-3091
PubMed: 19052360
DOI: 10.1107/S1744309108036373
Page generated: Wed Oct 28 07:58:42 2020

Last articles

Xe in 6AYK
Xe in 6QII
Xe in 6ASM
Xe in 5NSW
Xe in 6FY9
Xe in 5O1K
Xe in 5O27
Xe in 5M69
Xe in 5KPU
Xe in 5I63
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy