Bismuth in PDB 4h0w: Bismuth Bound Human Serum Transferrin

The structure of Bismuth Bound Human Serum Transferrin, PDB code: 4h0w was solved by N.Yang, H.Zhang, M.Wang, Q.Hao, H.Sun, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.95 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	73.907, 90.165, 111.032, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 25.6

The structure of Bismuth Bound Human Serum Transferrin also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Bismuth atom in the Bismuth Bound Human Serum Transferrin (pdb code 4h0w). This binding sites where shown within 5.0 Angstroms radius around Bismuth atom.
In total only one binding site of Bismuth was determined in the Bismuth Bound Human Serum Transferrin, PDB code: 4h0w:

Bismuth binding site 1 out of 1 in the Bismuth Bound Human Serum Transferrin


Mono view


Stereo pair view

A full contact list of Bismuth with other atoms in the Bi binding site number 1 of Bismuth Bound Human Serum Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Bi703 b:49.9 occ:0.70 OH A:TYR188 2.4 58.1 1.0 O4 A:NTA706 2.4 51.9 1.0 O13 A:NTA706 2.4 56.1 1.0 O3 A:CO3704 2.6 33.2 1.0 O A:HOH901 2.6 18.6 1.0 O2 A:CO3704 2.9 32.5 1.0 C2 A:NTA706 3.0 55.8 1.0 C3 A:NTA706 3.1 55.6 1.0 O8 A:NTA706 3.1 59.1 1.0 C A:CO3704 3.2 32.0 1.0 C7 A:NTA706 3.2 59.8 1.0 C11 A:NTA706 3.4 59.1 1.0 C6 A:NTA706 3.4 57.7 1.0 CZ A:TYR188 3.5 52.0 1.0 N1 A:NTA706 3.5 57.8 1.0 C10 A:NTA706 3.8 58.6 1.0 O9 A:NTA706 3.8 62.9 1.0 CE1 A:TYR188 4.0 47.2 1.0 NZ A:LYS206 4.0 47.7 1.0 O5 A:NTA706 4.3 55.1 1.0 CE A:LYS206 4.3 43.2 1.0 CD A:ARG124 4.4 41.6 1.0 NH1 A:ARG124 4.4 45.4 1.0 O1 A:CO3704 4.4 39.4 1.0 CE2 A:TYR188 4.5 54.0 1.0 O12 A:NTA706 4.6 56.5 1.0 N A:SER125 4.8 35.6 1.0 CB A:SER125 4.9 36.6 1.0

N.Yang, H.Zhang, M.Wang, Q.Hao, H.Sun. Iron and Bismuth Bound Human Serum Transferrin Reveals A Partially-Opened Conformation in the N-Lobe. Sci Rep V. 2 999 2012.
ISSN: ESSN 2045-2322
PubMed: 23256035
DOI: 10.1038/SREP00999