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Aluminium in PDB 3ar8: Calcium Pump Crystal Structure with Bound ALF4, Tnp-Amp and Tg

Enzymatic activity of Calcium Pump Crystal Structure with Bound ALF4, Tnp-Amp and Tg

All present enzymatic activity of Calcium Pump Crystal Structure with Bound ALF4, Tnp-Amp and Tg:
3.6.3.8;

Protein crystallography data

The structure of Calcium Pump Crystal Structure with Bound ALF4, Tnp-Amp and Tg, PDB code: 3ar8 was solved by C.Toyoshima, S.Yonekura, J.Tsueda, S.Iwasawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.99 / 2.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 176.864, 69.873, 141.813, 90.00, 106.71, 90.00
R / Rfree (%) 22.6 / 25.3

Other elements in 3ar8:

The structure of Calcium Pump Crystal Structure with Bound ALF4, Tnp-Amp and Tg also contains other interesting chemical elements:

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

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Calcium Pump Crystal Structure with Bound ALF4, Tnp-Amp and Tg (pdb code 3ar8). 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, Tnp-Amp and Tg, PDB code: 3ar8:

Aluminium binding site 1 out of 1 in 3ar8

Go back to Aluminium Binding Sites List in 3ar8
Aluminium binding site 1 out of 1 in the Calcium Pump Crystal Structure with Bound ALF4, Tnp-Amp and Tg


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, Tnp-Amp and Tg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al998

b:36.2
occ:1.00
AL A:ALF998 0.0 36.2 1.0
F1 A:ALF998 1.8 37.6 1.0
F2 A:ALF998 1.8 34.5 1.0
F4 A:ALF998 1.8 35.8 1.0
F3 A:ALF998 1.8 34.3 1.0
O A:HOH4003 1.9 26.9 1.0
OD2 A:ASP351 1.9 43.3 1.0
CG A:ASP351 2.9 45.3 1.0
OD1 A:ASP351 3.2 45.7 1.0
O A:HOH4002 3.4 37.8 1.0
OG1 A:THR625 3.6 44.2 1.0
MG A:MG995 3.7 37.3 1.0
NZ A:LYS684 3.9 39.0 1.0
O A:THR181 3.9 43.8 1.0
N A:THR353 3.9 43.9 1.0
N A:LYS352 4.0 41.2 1.0
OE2 A:GLU183 4.0 50.7 1.0
N A:GLY626 4.1 38.3 1.0
O A:HOH4001 4.3 36.1 1.0
CB A:ASP351 4.3 45.0 1.0
CB A:THR353 4.3 42.7 1.0
CA A:THR625 4.3 42.6 1.0
CA A:GLY182 4.3 40.4 1.0
ND2 A:ASN706 4.4 33.1 1.0
O A:THR353 4.4 45.9 1.0
CB A:THR625 4.4 41.6 1.0
CA A:THR353 4.6 42.9 1.0
O A:GLY182 4.6 41.9 1.0
OG1 A:THR353 4.7 36.5 1.0
C A:GLY182 4.7 42.6 1.0
CA A:ASP351 4.7 43.6 1.0
C A:LYS352 4.7 45.3 1.0
CA A:LYS352 4.8 41.4 1.0
OD1 A:ASP707 4.8 52.0 1.0
C A:THR625 4.8 44.2 1.0
C A:ASP351 4.8 42.3 1.0
C A:THR181 4.8 43.9 1.0
O A:ILE624 4.9 44.9 1.0
OD2 A:ASP707 4.9 55.9 1.0
CB A:LYS352 4.9 38.2 1.0
C A:THR353 5.0 44.5 1.0

Reference:

C.Toyoshima, S.Yonekura, J.Tsueda, S.Iwasawa. Trinitrophenyl Derivatives Bind Differently From Parent Adenine Nucleotides to CA2+-Atpase in the Absence of CA2+ Proc.Natl.Acad.Sci.Usa V. 108 1833 2011.
ISSN: ISSN 0027-8424
PubMed: 21239683
DOI: 10.1073/PNAS.1017659108
Page generated: Wed Jul 10 09:34:58 2024

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