Atomistry » Aluminium » PDB 5c2k-6i03 » 5xaa
Atomistry »
  Aluminium »
    PDB 5c2k-6i03 »
      5xaa »

Aluminium in PDB 5xaa: Complete Structure Factors and An Atomic Model of the Calcium Pump (SERCA1A) and Associated Phospholipids in the E2-Alf-(Tg) Crystals of P21212 Symmetry

Enzymatic activity of Complete Structure Factors and An Atomic Model of the Calcium Pump (SERCA1A) and Associated Phospholipids in the E2-Alf-(Tg) Crystals of P21212 Symmetry

All present enzymatic activity of Complete Structure Factors and An Atomic Model of the Calcium Pump (SERCA1A) and Associated Phospholipids in the E2-Alf-(Tg) Crystals of P21212 Symmetry:
3.6.3.8;

Protein crystallography data

The structure of Complete Structure Factors and An Atomic Model of the Calcium Pump (SERCA1A) and Associated Phospholipids in the E2-Alf-(Tg) Crystals of P21212 Symmetry, PDB code: 5xaa was solved by Y.Norimatsu, K.Hasegawa, N.Shimizu, C.Toyoshima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 91.56 / 3.20
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 120.900, 87.700, 140.200, 90.00, 90.00, 90.00
R / Rfree (%) 22.7 / 26

Other elements in 5xaa:

The structure of Complete Structure Factors and An Atomic Model of the Calcium Pump (SERCA1A) and Associated Phospholipids in the E2-Alf-(Tg) Crystals of P21212 Symmetry 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 Complete Structure Factors and An Atomic Model of the Calcium Pump (SERCA1A) and Associated Phospholipids in the E2-Alf-(Tg) Crystals of P21212 Symmetry (pdb code 5xaa). 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 Complete Structure Factors and An Atomic Model of the Calcium Pump (SERCA1A) and Associated Phospholipids in the E2-Alf-(Tg) Crystals of P21212 Symmetry, PDB code: 5xaa:

Aluminium binding site 1 out of 1 in 5xaa

Go back to Aluminium Binding Sites List in 5xaa
Aluminium binding site 1 out of 1 in the Complete Structure Factors and An Atomic Model of the Calcium Pump (SERCA1A) and Associated Phospholipids in the E2-Alf-(Tg) Crystals of P21212 Symmetry


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Complete Structure Factors and An Atomic Model of the Calcium Pump (SERCA1A) and Associated Phospholipids in the E2-Alf-(Tg) Crystals of P21212 Symmetry within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al1002

b:47.6
occ:1.00
AL A:ALF1002 0.0 47.6 1.0
F1 A:ALF1002 1.8 61.4 1.0
F3 A:ALF1002 1.8 64.3 1.0
F4 A:ALF1002 1.8 52.0 1.0
F2 A:ALF1002 1.8 45.2 1.0
OD1 A:ASP351 2.4 86.7 1.0
O A:HOH1108 2.6 53.6 1.0
OD2 A:ASP351 2.8 59.6 1.0
CG A:ASP351 2.9 70.6 1.0
O A:HOH1121 3.3 54.9 1.0
O A:THR181 3.6 54.5 1.0
MG A:MG1001 3.6 47.7 1.0
NZ A:LYS684 3.8 41.9 1.0
CA A:GLY182 3.8 56.0 1.0
ND2 A:ASN706 3.9 55.7 1.0
O A:HOH1104 4.0 59.0 1.0
OG1 A:THR625 4.0 62.1 1.0
N A:GLY626 4.2 49.5 1.0
O A:GLY182 4.2 56.5 1.0
N A:THR353 4.3 63.7 1.0
C A:GLY182 4.3 56.2 1.0
CB A:THR353 4.3 57.5 1.0
O A:THR353 4.4 73.4 1.0
CB A:ASP351 4.4 58.1 1.0
C A:THR181 4.5 55.0 1.0
OD1 A:ASP707 4.5 53.8 1.0
OE2 A:GLU183 4.6 54.6 1.0
N A:GLY182 4.6 55.7 1.0
N A:LYS352 4.6 69.1 1.0
OG1 A:THR353 4.6 53.1 1.0
CA A:THR625 4.6 54.9 1.0
OD2 A:ASP707 4.7 52.2 1.0
CA A:THR353 4.8 71.3 1.0
CB A:THR625 4.8 48.7 1.0
CG A:ASN706 4.8 68.9 1.0
OD1 A:ASN706 4.8 65.2 1.0
CE A:LYS684 4.9 49.0 1.0
C A:THR625 5.0 64.9 1.0

Reference:

Y.Norimatsu, K.Hasegawa, N.Shimizu, C.Toyoshima. Protein-Phospholipid Interplay Revealed with Crystals of A Calcium Pump. Nature V. 545 193 2017.
ISSN: ESSN 1476-4687
PubMed: 28467821
DOI: 10.1038/NATURE22357
Page generated: Sun Jul 6 21:58:11 2025

Last articles

Cl in 6APQ
Cl in 6AP6
Cl in 6AOL
Cl in 6AOK
Cl in 6ALZ
Cl in 6AOG
Cl in 6AOJ
Cl in 6ANG
Cl in 6AN4
Cl in 6ALE
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy