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Aluminium in PDB 4umw: Crystal Structure of A Zinc-Transporting Pib-Type Atpase in E2.Pi State

Enzymatic activity of Crystal Structure of A Zinc-Transporting Pib-Type Atpase in E2.Pi State

All present enzymatic activity of Crystal Structure of A Zinc-Transporting Pib-Type Atpase in E2.Pi State:
3.6.3.5;

Protein crystallography data

The structure of Crystal Structure of A Zinc-Transporting Pib-Type Atpase in E2.Pi State, PDB code: 4umw was solved by K.T.Wang, O.Sitsel, G.Meloni, H.E.Autzen, M.Andersson, T.Klymchuk, A.M.Nielsen, D.C.Rees, P.Nissen, P.Gourdon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.347 / 2.70
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 77.641, 83.560, 319.818, 90.00, 90.00, 90.00
R / Rfree (%) 22.43 / 24.06

Other elements in 4umw:

The structure of Crystal Structure of A Zinc-Transporting Pib-Type Atpase in E2.Pi State 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 Crystal Structure of A Zinc-Transporting Pib-Type Atpase in E2.Pi State (pdb code 4umw). 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 Crystal Structure of A Zinc-Transporting Pib-Type Atpase in E2.Pi State, PDB code: 4umw:

Aluminium binding site 1 out of 1 in 4umw

Go back to Aluminium Binding Sites List in 4umw
Aluminium binding site 1 out of 1 in the Crystal Structure of A Zinc-Transporting Pib-Type Atpase in E2.Pi State


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Crystal Structure of A Zinc-Transporting Pib-Type Atpase in E2.Pi State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al1731

b:47.0
occ:1.00
 AL A:ALF1731 0.0 47.0 1.0
F4 A:ALF1731 1.8 46.6 1.0
F1 A:ALF1731 1.8 56.2 1.0
F2 A:ALF1731 1.8 41.0 1.0
F3 A:ALF1731 1.8 42.1 1.0
OD1 A:ASP436 2.3 50.4 1.0
OD2 A:ASP436 2.9 48.5 1.0
CG A:ASP436 2.9 47.8 1.0
MG A:MG1732 3.1 45.0 1.0
O A:THR288 3.8 59.4 1.0
OG1 A:THR583 3.9 51.7 1.0
N A:THR438 4.0 44.3 1.0
NZ A:LYS610 4.0 46.0 1.0
N A:LYS437 4.1 48.2 1.0
CA A:GLY289 4.2 51.3 1.0
O A:THR438 4.3 45.3 1.0
CB A:THR438 4.3 46.4 1.0
O A:HOH2022 4.3 41.6 1.0
ND2 A:ASN631 4.3 42.3 1.0
N A:GLY584 4.3 49.5 1.0
CB A:ASP436 4.4 44.2 1.0
OE2 A:GLU290 4.5 62.6 1.0
CA A:THR438 4.6 44.8 1.0
OG1 A:THR438 4.6 44.3 1.0
C A:GLY289 4.6 54.3 1.0
CA A:THR583 4.6 52.4 1.0
O A:GLY289 4.7 57.7 1.0
CB A:THR583 4.7 51.5 1.0
C A:THR288 4.7 50.8 1.0
CA A:ASP436 4.8 43.5 1.0
C A:LYS437 4.8 44.9 1.0
CA A:LYS437 4.9 45.1 1.0
OD1 A:ASP632 4.9 45.5 1.0
C A:THR438 4.9 44.6 1.0
N A:GLY289 4.9 50.4 1.0
C A:ASP436 4.9 46.3 1.0
OD1 A:ASP628 5.0 47.8 1.0

Reference:

K.Wang, O.Sitsel, G.Meloni, H.E.Autzen, M.Andersson, T.Klymchuk, A.M.Nielsen, D.C.Rees, P.Nissen, P.Gourdon. Structure and Mechanism of Zn(2+)-Transporting P-Type Atpases. Nature V. 514 518 2014.
ISSN: ESSN 0028-0836
PubMed: 25132545
DOI: 10.1038/NATURE13618
Page generated: Sun Jul 6 21:55:14 2025

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