Zinc in PDB 5iih: Crystal Structure of Equine Serum Albumin in the Presence of 2.5 Mm Zinc at pH 7.4

The structure of Crystal Structure of Equine Serum Albumin in the Presence of 2.5 Mm Zinc at pH 7.4, PDB code: 5iih was solved by K.B.Handing, I.G.Shabalin, D.R.Cooper, S.C.Almo, W.Minor, New Yorkstructural Genomics Research Consortium (Nysgrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.01 / 2.40
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	93.098, 93.098, 141.442, 90.00, 90.00, 120.00
R / Rfree (%)	17.5 / 23.5

The binding sites of Zinc atom in the Crystal Structure of Equine Serum Albumin in the Presence of 2.5 Mm Zinc at pH 7.4 (pdb code 5iih). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Equine Serum Albumin in the Presence of 2.5 Mm Zinc at pH 7.4, PDB code: 5iih:

Zinc binding site 1 out of 1 in the Crystal Structure of Equine Serum Albumin in the Presence of 2.5 Mm Zinc at pH 7.4


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Equine Serum Albumin in the Presence of 2.5 Mm Zinc at pH 7.4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:73.9 occ:1.00 O A:HOH760 2.0 53.6 1.0 OD2 A:ASP248 2.0 88.2 1.0 ND1 A:HIS246 2.1 79.3 1.0 NE2 A:HIS67 2.1 83.4 1.0 CG A:ASP248 2.6 74.7 1.0 OD1 A:ASP248 2.6 87.5 1.0 CE1 A:HIS246 2.9 84.0 1.0 CE1 A:HIS67 3.0 76.3 1.0 CD2 A:HIS67 3.1 61.3 1.0 CG A:HIS246 3.2 82.0 1.0 CB A:HIS246 3.7 62.5 1.0 O A:HIS246 3.9 57.7 1.0 CB A:ASP248 4.0 77.2 1.0 NE2 A:HIS246 4.1 93.1 1.0 ND1 A:HIS67 4.2 66.0 1.0 CG A:HIS67 4.2 59.7 1.0 CD2 A:HIS246 4.2 84.5 1.0 ND2 A:ASN99 4.3 66.0 1.0 C A:HIS246 4.4 56.0 1.0 N A:ASP248 4.5 71.8 1.0 O A:HOH701 4.5 64.0 1.0 CA A:ASP248 4.6 59.5 1.0 CA A:HIS246 4.7 54.2 1.0

K.B.Handing, I.G.Shabalin, O.Kassaar, S.Khazaipoul, C.A.Blindauer, A.J.Stewart, M.Chruszcz, W.Minor. Circulatory Zinc Transport Is Controlled By Distinct Interdomain Sites on Mammalian Albumins. Chem Sci V. 7 6635 2016.
ISSN: ISSN 2041-6520
PubMed: 28567254
DOI: 10.1039/C6SC02267G