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Calcium in PDB 1su4: Crystal Structure of Calcium Atpase with Two Bound Calcium Ions

Enzymatic activity of Crystal Structure of Calcium Atpase with Two Bound Calcium Ions

All present enzymatic activity of Crystal Structure of Calcium Atpase with Two Bound Calcium Ions:
3.6.3.8;

Protein crystallography data

The structure of Crystal Structure of Calcium Atpase with Two Bound Calcium Ions, PDB code: 1su4 was solved by C.Toyoshima, M.Nakasako, H.Nomura, H.Ogawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 165.890, 64.340, 147.140, 90.00, 98.08, 90.00
R / Rfree (%) 24.6 / 28.3

Other elements in 1su4:

The structure of Crystal Structure of Calcium Atpase with Two Bound Calcium Ions also contains other interesting chemical elements:

Sodium (Na) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Calcium Atpase with Two Bound Calcium Ions (pdb code 1su4). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Calcium Atpase with Two Bound Calcium Ions, PDB code: 1su4:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1su4

Go back to Calcium Binding Sites List in 1su4
Calcium binding site 1 out of 2 in the Crystal Structure of Calcium Atpase with Two Bound Calcium Ions


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 Calcium Atpase with Two Bound Calcium Ions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca995

b:41.5
occ:1.00
OD1 A:ASN796 2.2 48.6 1.0
O A:ILE307 2.3 38.4 1.0
OD2 A:ASP800 2.3 38.4 1.0
OE1 A:GLU309 2.4 48.5 1.0
O A:VAL304 2.4 39.5 1.0
OE2 A:GLU309 2.6 45.4 1.0
O A:ALA305 2.7 38.1 1.0
CD A:GLU309 2.8 48.0 1.0
C A:ALA305 3.3 39.3 1.0
CG A:ASN796 3.4 49.5 1.0
CG A:ASP800 3.4 41.2 1.0
C A:ILE307 3.5 39.9 1.0
C A:VAL304 3.5 38.4 1.0
CA A:ALA305 3.6 39.9 1.0
CB A:ASP800 3.9 42.4 1.0
ND2 A:ASN796 4.0 46.9 1.0
N A:ALA305 4.0 40.4 1.0
OE2 A:GLU58 4.2 52.6 1.0
C A:ALA306 4.2 40.3 1.0
N A:ILE307 4.2 41.6 1.0
N A:ALA306 4.2 41.0 1.0
ND2 A:ASN768 4.3 39.7 1.0
O A:ALA306 4.3 39.0 1.0
O A:HOH2115 4.3 41.0 1.0
CA A:ILE307 4.3 37.8 1.0
CG A:GLU309 4.4 50.0 1.0
N A:PRO308 4.5 42.1 1.0
OD1 A:ASP800 4.5 44.2 1.0
N A:GLU309 4.6 46.5 1.0
CB A:ASN796 4.6 46.3 1.0
CB A:ILE307 4.6 39.0 1.0
CA A:PRO308 4.6 43.8 1.0
CA A:VAL304 4.8 36.7 1.0
CA A:ALA306 4.8 41.7 1.0
CG2 A:ILE307 4.9 41.4 1.0
CB A:ALA305 5.0 41.0 1.0
CG1 A:VAL304 5.0 30.9 1.0

Calcium binding site 2 out of 2 in 1su4

Go back to Calcium Binding Sites List in 1su4
Calcium binding site 2 out of 2 in the Crystal Structure of Calcium Atpase with Two Bound Calcium Ions


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 Calcium Atpase with Two Bound Calcium Ions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca996

b:44.3
occ:1.00
O A:HOH2115 2.3 41.0 1.0
O A:HOH2114 2.3 34.0 1.0
OD1 A:ASN768 2.3 36.5 1.0
OG1 A:THR799 2.4 45.2 1.0
OD1 A:ASP800 2.4 44.2 1.0
OE2 A:GLU771 2.4 44.7 1.0
OE1 A:GLU908 2.4 52.8 1.0
CB A:THR799 3.3 44.4 1.0
CG A:ASP800 3.4 41.2 1.0
CD A:GLU771 3.5 45.0 1.0
CD A:GLU908 3.5 52.7 1.0
CG A:ASN768 3.5 42.0 1.0
OE2 A:GLU908 3.8 55.1 1.0
OE1 A:GLU771 3.8 42.5 1.0
OD2 A:ASP800 3.9 38.4 1.0
C A:THR799 4.1 46.9 1.0
N A:ASP800 4.1 46.7 1.0
ND2 A:ASN768 4.2 39.7 1.0
CG2 A:THR799 4.3 46.6 1.0
CA A:THR799 4.3 46.3 1.0
O A:THR799 4.4 46.6 1.0
CB A:SER767 4.4 41.4 1.0
CG1 A:VAL795 4.5 49.2 1.0
CB A:ASP800 4.5 42.4 1.0
N A:ASN768 4.6 45.1 1.0
CA A:ASP800 4.7 46.7 1.0
CA A:ASN768 4.7 46.0 1.0
CB A:ASN768 4.7 40.2 1.0
CG A:GLU771 4.7 47.9 1.0
CG A:GLU908 4.8 51.4 1.0
O A:ALA305 4.8 38.1 1.0
O A:VAL795 4.9 48.1 1.0
C A:SER767 4.9 45.9 1.0

Reference:

C.Toyoshima, M.Nakasako, H.Nomura, H.Ogawa. Crystal Structure of the Calcium Pump of Sarcoplasmic Reticulum at 2.6 A Resolution Nature V. 405 647 2000.
ISSN: ISSN 0028-0836
PubMed: 10864315
DOI: 10.1038/35015017
Page generated: Thu Jul 11 22:50:08 2024

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