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Aluminium in PDB 5xja: The Crystal Structure of the Minimal Core Domain of the Microtubule Depolymerizer KIF2C Complexed with Adp-Mg-Alfx

Protein crystallography data

The structure of The Crystal Structure of the Minimal Core Domain of the Microtubule Depolymerizer KIF2C Complexed with Adp-Mg-Alfx, PDB code: 5xja was solved by T.Ogawa, X.Jiang, N.Hirokawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 3.43
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 91.098, 166.989, 74.991, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 23

Other elements in 5xja:

The structure of The Crystal Structure of the Minimal Core Domain of the Microtubule Depolymerizer KIF2C Complexed with Adp-Mg-Alfx also contains other interesting chemical elements:

Fluorine (F) 6 atoms
Magnesium (Mg) 2 atoms

Aluminium Binding Sites:

The binding sites of Aluminium atom in the The Crystal Structure of the Minimal Core Domain of the Microtubule Depolymerizer KIF2C Complexed with Adp-Mg-Alfx (pdb code 5xja). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the The Crystal Structure of the Minimal Core Domain of the Microtubule Depolymerizer KIF2C Complexed with Adp-Mg-Alfx, PDB code: 5xja:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in 5xja

Go back to Aluminium Binding Sites List in 5xja
Aluminium binding site 1 out of 2 in the The Crystal Structure of the Minimal Core Domain of the Microtubule Depolymerizer KIF2C Complexed with Adp-Mg-Alfx


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of The Crystal Structure of the Minimal Core Domain of the Microtubule Depolymerizer KIF2C Complexed with Adp-Mg-Alfx within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al603

b:34.8
occ:1.00
AL A:AF3603 0.0 34.8 1.0
F3 A:AF3603 1.9 36.9 1.0
F2 A:AF3603 1.9 32.1 1.0
F1 A:AF3603 1.9 32.3 1.0
O1B A:ADP602 2.3 54.2 1.0
OG1 A:THR351 2.6 39.2 1.0
MG A:MG601 2.9 1.0 1.0
OG A:SER463 3.5 54.2 1.0
PB A:ADP602 3.7 47.0 1.0
CB A:THR351 3.9 51.6 1.0
OD1 A:ASP488 4.0 42.6 1.0
OD2 A:ASP488 4.2 47.6 1.0
O2B A:ADP602 4.3 46.5 1.0
O3B A:ADP602 4.4 49.8 1.0
C A:SER463 4.5 56.0 1.0
N A:SER464 4.5 57.2 1.0
O2A A:ADP602 4.6 51.4 1.0
CG A:ASP488 4.6 45.5 1.0
OG A:SER464 4.6 69.7 1.0
O A:SER463 4.6 43.0 1.0
O3A A:ADP602 4.7 50.6 1.0
CG2 A:THR351 4.7 58.9 1.0
N A:THR351 4.7 53.5 1.0
CB A:SER463 4.8 52.3 1.0
CA A:THR351 4.9 54.2 1.0
NH1 A:ARG452 5.0 71.4 1.0
CA A:SER464 5.0 58.8 1.0

Aluminium binding site 2 out of 2 in 5xja

Go back to Aluminium Binding Sites List in 5xja
Aluminium binding site 2 out of 2 in the The Crystal Structure of the Minimal Core Domain of the Microtubule Depolymerizer KIF2C Complexed with Adp-Mg-Alfx


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of The Crystal Structure of the Minimal Core Domain of the Microtubule Depolymerizer KIF2C Complexed with Adp-Mg-Alfx within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Al603

b:35.0
occ:1.00
AL B:AF3603 0.0 35.0 1.0
F1 B:AF3603 1.9 34.3 1.0
F3 B:AF3603 1.9 34.7 1.0
F2 B:AF3603 1.9 33.9 1.0
MG B:MG601 2.3 58.4 1.0
O3B B:ADP602 2.4 46.3 1.0
OG1 B:THR351 2.6 39.5 1.0
PB B:ADP602 3.5 57.4 1.0
OG B:SER463 3.8 89.1 1.0
CB B:THR351 3.9 56.4 1.0
O2B B:ADP602 3.9 61.6 1.0
OD1 B:ASP488 4.1 35.5 1.0
O2A B:ADP602 4.4 57.0 1.0
OD2 B:ASP488 4.4 43.7 1.0
O1B B:ADP602 4.4 64.2 1.0
O B:SER463 4.5 80.5 1.0
C B:SER463 4.7 0.8 1.0
CG B:ASP488 4.7 40.9 1.0
CG2 B:THR351 4.7 60.6 1.0
N B:SER464 4.7 63.8 1.0
O3A B:ADP602 4.7 56.4 1.0
N B:THR351 4.8 59.0 1.0
NH2 B:ARG452 4.8 0.6 1.0
OG B:SER464 4.8 54.1 1.0
PA B:ADP602 4.8 51.8 1.0
CA B:THR351 4.9 56.6 1.0
CA B:SER464 5.0 51.9 1.0

Reference:

T.Ogawa, S.Saijo, N.Shimizu, X.Jiang, N.Hirokawa. Mechanism of Catalytic Microtubule Depolymerization Via KIF2-Tubulin Transitional Conformation Cell Rep V. 20 2626 2017.
ISSN: ESSN 2211-1247
PubMed: 28903043
DOI: 10.1016/J.CELREP.2017.08.067
Page generated: Sat Dec 12 01:34:09 2020

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