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Aluminium in PDB 2zbg: Calcium Pump Crystal Structure with Bound ALF4 and Tg in the Absence of Calcium

Enzymatic activity of Calcium Pump Crystal Structure with Bound ALF4 and Tg in the Absence of Calcium

All present enzymatic activity of Calcium Pump Crystal Structure with Bound ALF4 and Tg in the Absence of Calcium:
3.6.3.8;

Protein crystallography data

The structure of Calcium Pump Crystal Structure with Bound ALF4 and Tg in the Absence of Calcium, PDB code: 2zbg was solved by C.Toyoshima, H.Ogawa, Y.Norimatsu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 11.99 / 2.55
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 177.500, 70.200, 143.400, 90.00, 106.80, 90.00
R / Rfree (%) 22.4 / 24.8

Other elements in 2zbg:

The structure of Calcium Pump Crystal Structure with Bound ALF4 and Tg in the Absence of Calcium also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Magnesium (Mg) 1 atom

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Calcium Pump Crystal Structure with Bound ALF4 and Tg in the Absence of Calcium (pdb code 2zbg). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the Calcium Pump Crystal Structure with Bound ALF4 and Tg in the Absence of Calcium, PDB code: 2zbg:

Aluminium binding site 1 out of 1 in 2zbg

Go back to Aluminium Binding Sites List in 2zbg
Aluminium binding site 1 out of 1 in the Calcium Pump Crystal Structure with Bound ALF4 and Tg in the Absence of Calcium


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Calcium Pump Crystal Structure with Bound ALF4 and Tg in the Absence of Calcium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al998

b:38.1
occ:1.00
 AL A:ALF998 0.0 38.1 1.0
F1 A:ALF998 1.7 41.8 1.0
F4 A:ALF998 1.8 41.1 1.0
F2 A:ALF998 1.8 39.0 1.0
F3 A:ALF998 1.8 41.0 1.0
O A:HOH2037 2.0 34.3 1.0
OD2 A:ASP351 2.0 39.6 1.0
CG A:ASP351 3.0 43.1 1.0
OD1 A:ASP351 3.4 46.1 1.0
MG A:MG995 3.5 45.6 1.0
O A:HOH2018 3.6 43.8 1.0
OG1 A:THR625 3.6 46.7 1.0
O A:THR181 3.8 46.2 1.0
NZ A:LYS684 3.9 43.5 1.0
N A:THR353 4.0 48.1 1.0
N A:LYS352 4.0 45.6 1.0
N A:GLY626 4.1 37.9 1.0
OE2 A:GLU183 4.2 57.6 1.0
CA A:GLY182 4.3 46.7 1.0
ND2 A:ASN706 4.3 41.0 1.0
CB A:THR353 4.3 47.1 1.0
CA A:THR625 4.4 43.5 1.0
CB A:ASP351 4.4 43.9 1.0
O A:HOH2026 4.4 34.7 1.0
CB A:THR625 4.4 44.0 1.0
O A:THR353 4.5 48.9 1.0
O A:GLY182 4.6 48.9 1.0
CA A:THR353 4.6 48.0 1.0
C A:GLY182 4.7 48.6 1.0
OG1 A:THR353 4.7 42.9 1.0
CA A:ASP351 4.7 43.7 1.0
C A:LYS352 4.8 48.6 1.0
C A:THR625 4.8 43.4 1.0
C A:THR181 4.8 48.9 1.0
CA A:LYS352 4.8 44.6 1.0
OD1 A:ASP707 4.9 55.6 1.0
C A:ASP351 4.9 44.4 1.0
O A:ILE624 4.9 46.1 1.0
CB A:LYS352 5.0 40.8 1.0
OD2 A:ASP707 5.0 58.2 1.0

Reference:

C.Toyoshima, Y.Norimatsu, S.Iwasawa, T.Tsuda, H.Ogawa. How Processing of Aspartylphosphate Is Coupled to Lumenal Gating of the Ion Pathway in the Calcium Pump Proc.Natl.Acad.Sci.Usa V. 104 19831 2007.
ISSN: ISSN 0027-8424
PubMed: 18077416
DOI: 10.1073/PNAS.0709978104
Page generated: Wed Jul 10 09:34:21 2024

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