Calcium in PDB 3s9n: Complex Between Transferrin Receptor 1 and Transferrin with Iron in the N-Lobe, Room Temperature

The structure of Complex Between Transferrin Receptor 1 and Transferrin with Iron in the N-Lobe, Room Temperature, PDB code: 3s9n was solved by B.E.Eckenroth, A.N.Steere, A.B.Mason, S.J.Everse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 3.25
Space group	P 43 2 2
Cell size a, b, c (Å), α, β, γ (°)	234.417, 234.417, 169.650, 90.00, 90.00, 90.00
R / Rfree (%)	25.4 / 28.9

The structure of Complex Between Transferrin Receptor 1 and Transferrin with Iron in the N-Lobe, Room Temperature also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Calcium atom in the Complex Between Transferrin Receptor 1 and Transferrin with Iron in the N-Lobe, Room Temperature (pdb code 3s9n). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Complex Between Transferrin Receptor 1 and Transferrin with Iron in the N-Lobe, Room Temperature, PDB code: 3s9n:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Complex Between Transferrin Receptor 1 and Transferrin with Iron in the N-Lobe, Room Temperature


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Complex Between Transferrin Receptor 1 and Transferrin with Iron in the N-Lobe, Room Temperature within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca900 b:96.0 occ:1.00 OE2 A:GLU465 2.1 70.7 1.0 O A:PHE313 2.1 56.4 1.0 O A:THR310 2.1 65.2 1.0 OE1 A:GLU468 2.2 63.6 1.0 OE1 A:GLU465 2.4 70.7 1.0 CD A:GLU465 2.5 70.7 1.0 OG1 A:THR310 2.7 51.7 1.0 C A:PHE313 3.2 56.4 1.0 C A:THR310 3.3 65.2 1.0 CB A:THR310 3.5 51.7 1.0 CD A:GLU468 3.5 63.6 1.0 CA A:PRO314 3.9 67.7 1.0 N A:PRO314 4.0 67.7 1.0 CA A:THR310 4.0 65.2 1.0 CG A:GLU465 4.1 70.7 1.0 C A:PRO314 4.2 67.7 1.0 OE2 A:GLU468 4.2 63.6 1.0 N A:PHE313 4.2 56.4 1.0 N A:SER315 4.3 58.8 1.0 N A:PRO311 4.3 74.4 1.0 CA A:PHE313 4.4 56.4 1.0 OG A:SER315 4.4 51.7 1.0 O A:ASP307 4.5 66.5 1.0 CB A:GLU468 4.5 63.6 1.0 CG A:GLU468 4.5 63.6 1.0 N A:GLY312 4.6 75.8 1.0 CA A:PRO311 4.6 74.4 1.0 CB A:ASP307 4.7 76.8 1.0 CA A:GLU465 4.8 64.1 1.0 O A:PRO314 4.8 67.7 1.0 C A:PRO311 4.8 74.4 1.0 CB A:GLU465 4.8 70.7 1.0 CG2 A:THR310 4.8 51.7 1.0 C A:GLY312 4.9 75.8 1.0 N A:ASP307 4.9 66.5 1.0 N A:THR310 4.9 65.2 1.0

Calcium binding site 2 out of 2 in the Complex Between Transferrin Receptor 1 and Transferrin with Iron in the N-Lobe, Room Temperature


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Complex Between Transferrin Receptor 1 and Transferrin with Iron in the N-Lobe, Room Temperature within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca900 b:96.0 occ:1.00 OE1 B:GLU468 2.1 68.7 1.0 O B:THR310 2.1 45.0 1.0 O B:PHE313 2.2 73.1 1.0 OE1 B:GLU465 2.4 70.6 1.0 OG1 B:THR310 2.4 28.2 1.0 OE2 B:GLU465 2.5 70.6 1.0 CD B:GLU465 2.8 70.6 1.0 C B:PHE313 3.2 73.1 1.0 C B:THR310 3.3 45.0 1.0 CD B:GLU468 3.3 68.7 1.0 CB B:THR310 3.4 28.2 1.0 CA B:PRO314 3.8 65.2 1.0 OE2 B:GLU468 3.8 68.7 1.0 N B:PRO314 3.9 65.2 1.0 CA B:THR310 4.0 45.0 1.0 C B:PRO314 4.0 65.2 1.0 N B:PHE313 4.1 73.1 1.0 OG B:SER315 4.2 52.0 1.0 CA B:PHE313 4.3 73.1 1.0 CG B:GLU465 4.3 70.6 1.0 N B:PRO311 4.3 79.2 1.0 O B:PRO314 4.4 65.2 1.0 N B:SER315 4.4 82.2 1.0 N B:GLY312 4.4 70.7 1.0 CG B:GLU468 4.5 68.7 1.0 CB B:GLU468 4.5 68.7 1.0 O B:ASP307 4.6 83.9 1.0 CA B:PRO311 4.6 79.2 1.0 C B:GLY312 4.6 70.7 1.0 C B:PRO311 4.7 79.2 1.0 CG2 B:THR310 4.8 28.2 1.0 N B:THR310 4.9 45.0 1.0 CB B:ASP307 4.9 80.1 1.0 CB B:GLU465 4.9 70.6 1.0 CA B:GLU465 5.0 82.8 1.0

B.E.Eckenroth, A.N.Steere, N.D.Chasteen, S.J.Everse, A.B.Mason. How the Binding of Human Transferrin Primes the Transferrin Receptor Potentiating Iron Release at Endosomal pH. Proc.Natl.Acad.Sci.Usa V. 108 13089 2011.
ISSN: ISSN 0027-8424
PubMed: 21788477
DOI: 10.1073/PNAS.1105786108