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Calcium in PDB 1anw: The Effect of Metal Binding on the Structure of Annexin V and Implications For Membrane Binding

Protein crystallography data

The structure of The Effect of Metal Binding on the Structure of Annexin V and Implications For Membrane Binding, PDB code: 1anw was solved by A.Lewit-Bentley, S.Morera, R.Huber, G.Bodo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 12.00 / 2.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 83.900, 80.900, 71.400, 90.00, 108.70, 90.00
R / Rfree (%) n/a / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the The Effect of Metal Binding on the Structure of Annexin V and Implications For Membrane Binding (pdb code 1anw). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the The Effect of Metal Binding on the Structure of Annexin V and Implications For Membrane Binding, PDB code: 1anw:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in 1anw

Go back to Calcium Binding Sites List in 1anw
Calcium binding site 1 out of 4 in the The Effect of Metal Binding on the Structure of Annexin V and Implications For Membrane Binding


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Effect of Metal Binding on the Structure of Annexin V and Implications For Membrane Binding within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca351

b:15.2
occ:1.00
O A:HOH823 2.3 25.6 1.0
O A:GLY30 2.3 18.9 1.0
OE2 A:GLU72 2.3 14.0 1.0
O A:MET28 2.3 16.7 1.0
O A:GLY32 2.4 9.7 1.0
OE1 A:GLU72 2.7 13.7 1.0
CD A:GLU72 2.8 14.3 1.0
C A:MET28 3.5 16.8 1.0
C A:GLY32 3.5 10.5 1.0
C A:GLY30 3.6 18.7 1.0
N A:GLY32 3.9 13.6 1.0
CA A:MET28 4.1 16.2 1.0
OG1 A:THR33 4.2 8.9 1.0
C A:LEU31 4.2 15.4 1.0
CG A:GLU72 4.3 12.7 1.0
CA A:GLY32 4.4 11.4 1.0
N A:GLY30 4.4 19.2 1.0
N A:LEU31 4.4 17.8 1.0
CA A:LEU31 4.5 16.9 1.0
C A:LYS29 4.5 18.9 1.0
N A:THR33 4.6 9.9 1.0
N A:LYS29 4.6 17.7 1.0
CB A:MET28 4.6 15.6 1.0
O A:LYS29 4.6 19.0 1.0
CA A:GLY30 4.6 18.6 1.0
O A:LEU31 4.8 16.0 1.0
O A:HOH749 4.9 34.4 1.0
CA A:LYS29 4.9 18.4 1.0
CA A:THR33 5.0 9.6 1.0

Calcium binding site 2 out of 4 in 1anw

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Calcium binding site 2 out of 4 in the The Effect of Metal Binding on the Structure of Annexin V and Implications For Membrane Binding


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The Effect of Metal Binding on the Structure of Annexin V and Implications For Membrane Binding within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca352

b:29.4
occ:1.00
O A:HOH981 1.8 29.4 1.0
O A:GLY263 2.1 20.1 1.0
O A:GLY261 2.2 31.2 1.0
O A:MET259 2.2 22.8 1.0
OD2 A:ASP303 2.8 17.6 1.0
OD1 A:ASP303 3.0 16.9 1.0
O A:HOH902 3.0 40.4 1.0
C A:GLY261 3.1 30.1 1.0
CG A:ASP303 3.2 16.3 1.0
C A:GLY263 3.3 20.7 1.0
C A:MET259 3.4 22.2 1.0
N A:GLY263 3.6 25.3 1.0
N A:ALA262 3.8 29.9 1.0
C A:ALA262 3.9 27.1 1.0
N A:GLY261 3.9 28.8 1.0
CA A:GLY261 4.1 29.6 1.0
CA A:GLY263 4.1 22.6 1.0
CA A:MET259 4.1 20.6 1.0
CA A:ALA262 4.1 28.5 1.0
C A:LYS260 4.2 27.9 1.0
N A:THR264 4.3 18.7 1.0
OG1 A:THR264 4.3 19.4 1.0
N A:LYS260 4.4 24.3 1.0
O A:HOH938 4.5 51.3 1.0
O A:ALA262 4.5 26.8 1.0
O A:LYS260 4.6 28.2 1.0
O A:HOH980 4.6 44.9 1.0
CA A:THR264 4.7 17.4 1.0
CB A:MET259 4.7 18.2 1.0
CB A:ASP303 4.7 14.9 1.0
CA A:LYS260 4.7 26.9 1.0

Calcium binding site 3 out of 4 in 1anw

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Calcium binding site 3 out of 4 in the The Effect of Metal Binding on the Structure of Annexin V and Implications For Membrane Binding


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of The Effect of Metal Binding on the Structure of Annexin V and Implications For Membrane Binding within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca353

b:26.3
occ:1.00
O B:HOH861 2.2 21.4 1.0
O B:HOH757 2.3 39.2 1.0
O B:MET28 2.4 21.7 1.0
O B:GLY32 2.4 24.6 1.0
O B:GLY30 2.5 29.0 1.0
OE1 B:GLU72 2.5 23.6 1.0
OE2 B:GLU72 2.5 22.2 1.0
CD B:GLU72 2.9 21.2 1.0
C B:GLY32 3.5 25.1 1.0
C B:MET28 3.6 22.2 1.0
C B:GLY30 3.7 28.8 1.0
N B:GLY32 3.7 28.2 1.0
OG1 B:THR33 4.0 21.9 1.0
CA B:MET28 4.2 21.4 1.0
CA B:GLY32 4.2 26.4 1.0
C B:LEU31 4.2 29.4 1.0
CG B:GLU72 4.4 20.2 1.0
N B:GLY30 4.4 26.6 1.0
C B:LYS29 4.5 25.1 1.0
N B:THR33 4.5 23.8 1.0
N B:LEU31 4.6 29.7 1.0
CA B:LEU31 4.6 30.0 1.0
N B:LYS29 4.6 23.2 1.0
CA B:GLY30 4.6 28.0 1.0
O B:LYS29 4.7 25.0 1.0
CB B:MET28 4.7 21.2 1.0
O B:HOH785 4.7 33.4 1.0
CA B:THR33 4.8 22.2 1.0
CA B:LYS29 4.9 24.2 1.0
O B:LEU31 4.9 30.6 1.0
O B:HOH984 4.9 41.5 1.0

Calcium binding site 4 out of 4 in 1anw

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Calcium binding site 4 out of 4 in the The Effect of Metal Binding on the Structure of Annexin V and Implications For Membrane Binding


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of The Effect of Metal Binding on the Structure of Annexin V and Implications For Membrane Binding within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca354

b:26.7
occ:1.00
O B:GLY261 2.4 29.7 1.0
O B:MET259 2.4 21.0 1.0
OD2 B:ASP303 2.5 14.8 1.0
O B:GLY263 2.6 22.8 1.0
O B:HOH891 2.7 46.8 1.0
OD1 B:ASP303 2.7 15.0 1.0
CG B:ASP303 2.9 14.8 1.0
C B:GLY261 3.5 29.0 1.0
C B:GLY263 3.6 23.0 1.0
C B:MET259 3.6 21.4 1.0
N B:GLY263 3.9 26.2 1.0
C B:ALA262 4.1 27.1 1.0
N B:GLY261 4.2 27.5 1.0
CB B:ASP303 4.4 14.0 1.0
CA B:MET259 4.4 19.7 1.0
N B:ALA262 4.4 28.9 1.0
CA B:GLY263 4.4 24.3 1.0
C B:LYS260 4.4 27.0 1.0
OG1 B:THR264 4.4 21.0 1.0
CA B:ALA262 4.4 27.9 1.0
CA B:GLY261 4.5 28.5 1.0
O B:HOH912 4.6 22.0 1.0
N B:THR264 4.6 21.4 1.0
N B:LYS260 4.7 23.7 1.0
O B:ALA262 4.7 27.4 1.0
O B:LYS260 4.7 26.9 1.0
CA B:LYS260 4.8 26.6 1.0
CB B:MET259 4.8 17.9 1.0
O B:HOH910 4.9 23.8 1.0
CA B:THR264 5.0 20.2 1.0
CA B:ASP303 5.0 13.4 1.0

Reference:

A.Lewit-Bentley, S.Morera, R.Huber, G.Bodo. The Effect of Metal Binding on the Structure of Annexin V and Implications For Membrane Binding. Eur.J.Biochem. V. 210 73 1992.
ISSN: ISSN 0014-2956
PubMed: 1446685
DOI: 10.1111/J.1432-1033.1992.TB17392.X
Page generated: Thu Jul 11 05:59:46 2024

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