Calcium in PDB 4j3h: Ring Cycle For Dilating and Constricting the Nuclear Pore: Structure of A NUP54 Homo-Tetramer.

The structure of Ring Cycle For Dilating and Constricting the Nuclear Pore: Structure of A NUP54 Homo-Tetramer., PDB code: 4j3h was solved by S.R.Solmaz, G.Blobel, I.Melcak, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.66 / 1.50
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	41.320, 41.320, 198.410, 90.00, 90.00, 120.00
R / Rfree (%)	19.2 / 22.3

The binding sites of Calcium atom in the Ring Cycle For Dilating and Constricting the Nuclear Pore: Structure of A NUP54 Homo-Tetramer. (pdb code 4j3h). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Ring Cycle For Dilating and Constricting the Nuclear Pore: Structure of A NUP54 Homo-Tetramer., PDB code: 4j3h:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Ring Cycle For Dilating and Constricting the Nuclear Pore: Structure of A NUP54 Homo-Tetramer.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Ring Cycle For Dilating and Constricting the Nuclear Pore: Structure of A NUP54 Homo-Tetramer. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca501 b:18.6 occ:1.00 OD1 A:ASP490 2.3 16.1 1.0 O A:ASP487 2.4 14.9 1.0 OD1 A:ASP487 2.4 22.7 1.0 CG A:ASP490 3.4 13.6 1.0 C A:ASP487 3.4 14.3 1.0 CG A:ASP487 3.6 26.4 1.0 OD2 A:ASP490 3.8 15.1 1.0 CA A:ASP487 3.8 15.2 1.0 O B:HOH609 3.9 26.4 1.0 CB A:ASP487 4.3 15.6 1.0 O A:HOH631 4.4 33.0 1.0 H2 B:HOH609 4.6 31.7 1.0 OD2 A:ASP487 4.6 38.2 1.0 N A:LEU488 4.6 15.2 1.0 CB A:ASP490 4.6 13.7 1.0 H1 B:HOH609 4.7 31.7 1.0 O A:ASP486 4.8 18.4 1.0 H1 A:HOH631 5.0 39.6 1.0

Calcium binding site 2 out of 3 in the Ring Cycle For Dilating and Constricting the Nuclear Pore: Structure of A NUP54 Homo-Tetramer.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Ring Cycle For Dilating and Constricting the Nuclear Pore: Structure of A NUP54 Homo-Tetramer. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca502 b:17.3 occ:1.00 O A:HOH605 2.5 27.9 1.0 O A:HOH639 2.5 42.5 1.0 OD1 A:ASP459 2.6 21.0 1.0 OD2 A:ASP459 2.6 24.9 1.0 O A:HOH601 2.6 26.3 1.0 CG A:ASP459 2.9 24.6 1.0 H2 A:HOH605 3.1 33.4 1.0 H2 A:HOH601 3.2 31.5 1.0 H1 A:HOH605 3.3 33.4 1.0 H1 A:HOH603 3.3 26.4 1.0 H1 A:HOH639 3.3 51.0 1.0 H2 A:HOH639 3.3 51.0 1.0 H1 A:HOH601 3.4 31.5 1.0 H1 A:HOH632 3.8 25.5 1.0 O A:HOH603 4.2 22.0 1.0 O A:HOH641 4.4 39.4 1.0 CB A:ASP459 4.4 17.0 1.0 O A:HOH632 4.4 21.2 1.0 H2 A:HOH632 4.5 25.5 1.0 H1 A:HOH636 4.6 50.0 1.0 H1 A:HOH641 4.6 47.2 1.0 H2 A:HOH603 4.9 26.4 1.0 O A:HOH636 5.0 41.7 1.0

Calcium binding site 3 out of 3 in the Ring Cycle For Dilating and Constricting the Nuclear Pore: Structure of A NUP54 Homo-Tetramer.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Ring Cycle For Dilating and Constricting the Nuclear Pore: Structure of A NUP54 Homo-Tetramer. within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca501 b:14.4 occ:1.00 O B:ILE483 2.2 15.1 1.0 O B:HOH604 2.4 18.3 1.0 OD2 B:ASP487 2.4 19.4 1.0 OD1 B:ASP486 2.4 21.4 1.0 H1 B:HOH604 3.2 22.0 1.0 H2 B:HOH604 3.2 22.0 1.0 CG B:ASP486 3.3 22.6 1.0 CG B:ASP487 3.4 18.8 1.0 C B:ILE483 3.5 13.6 1.0 OD2 B:ASP486 3.5 23.9 1.0 H1 A:HOH634 3.7 25.5 1.0 OD1 B:ASP487 3.8 20.4 1.0 O B:HOH603 4.1 19.6 1.0 H2 B:HOH603 4.3 23.6 1.0 N B:ILE484 4.4 15.1 1.0 CA B:ILE483 4.4 15.6 1.0 CA B:ILE484 4.5 17.1 1.0 N B:ASP487 4.5 23.3 1.0 CB B:ASP487 4.6 20.7 1.0 O A:HOH634 4.7 21.2 1.0 CB B:ASP486 4.7 26.0 1.0 CG2 B:ILE483 4.7 13.5 1.0 C B:ILE484 4.8 17.9 1.0 N B:ASP486 4.9 24.1 1.0 H1 B:HOH603 4.9 23.6 1.0 C B:ASP486 5.0 26.2 1.0

S.R.Solmaz, G.Blobel, I.Melcak. Ring Cycle For Dilating and Constricting the Nuclear Pore. Proc.Natl.Acad.Sci.Usa V. 110 5858 2013.
ISSN: ISSN 0027-8424
PubMed: 23479651
DOI: 10.1073/PNAS.1302655110