Iron in PDB 2pms: Crystal Structure of the Complex of Human Lactoferrin N-Lobe and Lactoferrin-Binding Domain of Pneumococcal Surface Protein A

The structure of Crystal Structure of the Complex of Human Lactoferrin N-Lobe and Lactoferrin-Binding Domain of Pneumococcal Surface Protein A, PDB code: 2pms was solved by D.Chattopadhyay, O.Senkovich, W.J.Cook, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 2.91
Space group	P 32
Cell size a, b, c (Å), α, β, γ (°)	130.180, 130.180, 80.800, 90.00, 90.00, 120.00
R / Rfree (%)	20.3 / 24.9

The structure of Crystal Structure of the Complex of Human Lactoferrin N-Lobe and Lactoferrin-Binding Domain of Pneumococcal Surface Protein A also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Iron atom in the Crystal Structure of the Complex of Human Lactoferrin N-Lobe and Lactoferrin-Binding Domain of Pneumococcal Surface Protein A (pdb code 2pms). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of the Complex of Human Lactoferrin N-Lobe and Lactoferrin-Binding Domain of Pneumococcal Surface Protein A, PDB code: 2pms:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the Complex of Human Lactoferrin N-Lobe and Lactoferrin-Binding Domain of Pneumococcal Surface Protein A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of the Complex of Human Lactoferrin N-Lobe and Lactoferrin-Binding Domain of Pneumococcal Surface Protein A within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe347 b:18.6 occ:1.00 O1 A:CO3346 1.8 21.1 1.0 OH A:TYR193 1.9 27.4 1.0 OD1 A:ASP61 1.9 25.2 1.0 OH A:TYR93 2.1 20.7 1.0 NE2 A:HIS254 2.2 21.2 1.0 C A:CO3346 2.6 21.4 1.0 O2 A:CO3346 2.7 21.2 1.0 CZ A:TYR193 3.0 27.5 1.0 CG A:ASP61 3.1 23.8 1.0 CZ A:TYR93 3.1 19.9 1.0 CE1 A:HIS254 3.1 21.5 1.0 CD2 A:HIS254 3.3 20.9 1.0 CE2 A:TYR93 3.6 18.9 1.0 CE1 A:TYR193 3.7 27.5 1.0 O3 A:CO3346 3.8 21.7 1.0 CB A:ASP61 3.9 22.1 1.0 CE2 A:TYR193 3.9 27.1 1.0 NH2 A:ARG211 4.0 29.4 1.0 OD2 A:ASP61 4.0 26.2 1.0 CE1 A:TYR93 4.1 19.9 1.0 ND1 A:HIS254 4.3 20.9 1.0 CB A:THR123 4.3 26.2 1.0 CG A:HIS254 4.4 20.8 1.0 CA A:ASP61 4.6 21.6 1.0 OG1 A:THR123 4.6 26.9 1.0 N A:ALA124 4.8 25.5 1.0 N A:THR123 4.8 26.5 1.0 NE A:ARG122 4.9 34.8 1.0 N A:GLY62 4.9 21.8 1.0 CD2 A:TYR93 4.9 19.9 1.0 CZ A:ARG211 4.9 30.2 1.0 NE A:ARG211 5.0 29.1 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the Complex of Human Lactoferrin N-Lobe and Lactoferrin-Binding Domain of Pneumococcal Surface Protein A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of the Complex of Human Lactoferrin N-Lobe and Lactoferrin-Binding Domain of Pneumococcal Surface Protein A within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe347 b:18.7 occ:1.00 OH B:TYR193 1.8 27.1 1.0 O1 B:CO3346 1.9 21.3 1.0 OD1 B:ASP61 1.9 25.4 1.0 OH B:TYR93 2.1 20.4 1.0 NE2 B:HIS254 2.2 20.1 1.0 O2 B:CO3346 2.6 21.4 1.0 C B:CO3346 2.6 21.6 1.0 CZ B:TYR193 3.0 27.3 1.0 CE1 B:HIS254 3.0 20.7 1.0 CZ B:TYR93 3.1 20.1 1.0 CG B:ASP61 3.1 24.1 1.0 CD2 B:HIS254 3.2 20.8 1.0 CE2 B:TYR93 3.7 19.6 1.0 CE1 B:TYR193 3.7 27.6 1.0 O3 B:CO3346 3.8 22.2 1.0 CE2 B:TYR193 3.9 27.0 1.0 CB B:ASP61 4.0 22.1 1.0 OD2 B:ASP61 4.0 26.9 1.0 NH2 B:ARG211 4.1 28.8 1.0 CE1 B:TYR93 4.2 19.8 1.0 ND1 B:HIS254 4.2 20.6 1.0 CB B:THR123 4.3 26.5 1.0 CG B:HIS254 4.3 20.7 1.0 OG1 B:THR123 4.6 27.3 1.0 CA B:ASP61 4.7 21.8 1.0 N B:ALA124 4.7 25.8 1.0 N B:THR123 4.8 27.0 1.0 NE B:ARG122 4.9 35.6 1.0 NE B:ARG211 4.9 29.7 1.0 CZ B:ARG211 5.0 30.3 1.0 CD2 B:TYR93 5.0 19.7 1.0

O.Senkovich, W.J.Cook, S.Mirza, S.K.Hollingshead, I.I.Protasevich, D.E.Briles, D.Chattopadhyay. Structure of A Complex of Human Lactoferrin N-Lobe with Pneumococcal Surface Protein A Provides Insight Into Microbial Defense Mechanism. J.Mol.Biol. V. 370 701 2007.
ISSN: ISSN 0022-2836
PubMed: 17543335
DOI: 10.1016/J.JMB.2007.04.075