Zinc in PDB 3li2: Closed Conformation of Htsa Complexed with Staphyloferrin A

The structure of Closed Conformation of Htsa Complexed with Staphyloferrin A, PDB code: 3li2 was solved by J.C.Grigg, M.E.P.Murphy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.15 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.280, 148.600, 52.270, 90.00, 117.14, 90.00
R / Rfree (%)	16.5 / 21.6

The structure of Closed Conformation of Htsa Complexed with Staphyloferrin A also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Zinc atom in the Closed Conformation of Htsa Complexed with Staphyloferrin A (pdb code 3li2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Closed Conformation of Htsa Complexed with Staphyloferrin A, PDB code: 3li2:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Closed Conformation of Htsa Complexed with Staphyloferrin A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Closed Conformation of Htsa Complexed with Staphyloferrin A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:33.8 occ:1.00 NE2 A:HIS266 1.8 29.0 1.0 O A:HOH404 2.2 34.0 1.0 CE1 A:HIS266 2.6 30.6 1.0 CD2 A:HIS266 2.9 28.2 1.0 O A:HOH363 3.0 47.2 1.0 ND1 A:HIS266 3.8 30.3 1.0 CG A:HIS266 4.0 28.1 1.0 OG A:SER271 4.1 49.0 1.0 O A:HOH331 4.6 23.2 1.0 O A:HOH414 4.6 36.5 1.0 CB A:SER271 4.7 46.9 1.0 CA A:SER271 5.0 47.8 1.0

Zinc binding site 2 out of 4 in the Closed Conformation of Htsa Complexed with Staphyloferrin A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Closed Conformation of Htsa Complexed with Staphyloferrin A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2 b:26.1 occ:1.00 OD1 A:ASP270 1.7 38.6 1.0 ND1 A:HIS266 2.4 30.3 1.0 CG A:ASP270 2.6 46.2 1.0 OD2 A:ASP270 2.8 45.9 1.0 CG A:HIS266 3.0 28.1 1.0 CB A:HIS266 3.2 28.0 1.0 CE1 A:HIS266 3.4 30.6 1.0 N A:SER271 3.9 47.1 1.0 CB A:ASP270 4.1 48.7 1.0 CD2 A:HIS266 4.2 28.2 1.0 CA A:HIS266 4.3 27.8 1.0 NE2 A:HIS266 4.4 29.0 1.0 N A:ASP270 4.5 46.1 1.0 CA A:ASP270 4.6 47.0 1.0 CB A:LYS268 4.6 47.9 1.0 CA A:SER271 4.6 47.8 1.0 C A:ASP270 4.8 46.8 1.0 N A:LYS268 4.9 45.6 1.0 C A:HIS266 4.9 28.1 1.0

Zinc binding site 3 out of 4 in the Closed Conformation of Htsa Complexed with Staphyloferrin A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Closed Conformation of Htsa Complexed with Staphyloferrin A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn3 b:24.0 occ:1.00 OD1 A:ASP248 1.8 23.5 1.0 ND1 A:HIS251 2.1 30.8 1.0 OD2 A:ASP248 2.4 31.3 1.0 CG A:ASP248 2.4 28.7 1.0 CG A:HIS251 3.0 29.1 1.0 CE1 A:HIS251 3.1 32.2 1.0 CB A:HIS251 3.3 27.1 1.0 N A:HIS251 3.4 28.3 1.0 CA A:HIS251 3.6 28.0 1.0 O A:HOH416 3.6 25.3 1.0 CB A:ASP248 3.9 29.5 1.0 CD2 A:HIS251 4.1 27.8 1.0 NE2 A:HIS251 4.2 31.6 1.0 C A:GLU250 4.3 30.1 1.0 N A:ASP248 4.7 28.2 1.0 CA A:ASP248 4.8 29.0 1.0 CB A:GLU250 4.9 33.1 1.0

Zinc binding site 4 out of 4 in the Closed Conformation of Htsa Complexed with Staphyloferrin A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Closed Conformation of Htsa Complexed with Staphyloferrin A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn4 b:34.8 occ:1.00 OD2 A:ASP254 2.2 34.6 1.0 OD1 A:ASP254 2.3 34.7 1.0 CG A:ASP254 2.6 34.7 1.0 O A:HOH373 3.4 34.0 1.0 CB A:ASP254 4.1 33.3 1.0 O A:GLU250 4.2 30.5 1.0 OE1 A:GLU250 4.5 41.8 1.0 C A:GLU250 4.9 30.1 1.0

J.C.Grigg, J.D.Cooper, J.Cheung, D.E.Heinrichs, M.E.Murphy. The Staphylococcus Aureus Siderophore Receptor Htsa Undergoes Localized Conformational Changes to Enclose Staphyloferrin A in An Arginine-Rich Binding Pocket. J.Biol.Chem. V. 285 11162 2010.
ISSN: ISSN 0021-9258
PubMed: 20147287
DOI: 10.1074/JBC.M109.097865