Iron in PDB 2q7a: Crystal Structure of the Cell Surface Heme Transfer Protein Shp

The structure of Crystal Structure of the Cell Surface Heme Transfer Protein Shp, PDB code: 2q7a was solved by R.Aranda Iv, C.E.Worley, E.Bitto, G.N.Phillips Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.17 / 2.10
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	82.317, 82.317, 106.054, 90.00, 90.00, 120.00
R / Rfree (%)	16.3 / 22.2

The binding sites of Iron atom in the Crystal Structure of the Cell Surface Heme Transfer Protein Shp (pdb code 2q7a). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of the Cell Surface Heme Transfer Protein Shp, PDB code: 2q7a:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of the Cell Surface Heme Transfer Protein Shp


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 Cell Surface Heme Transfer Protein Shp within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe182 b:27.1 occ:1.00 FE A:HEM182 0.0 27.1 1.0 ND A:HEM182 2.0 26.8 1.0 NA A:HEM182 2.1 26.1 1.0 NC A:HEM182 2.1 26.5 1.0 NB A:HEM182 2.1 24.6 1.0 O1A B:HEM181 3.0 37.3 1.0 C4D A:HEM182 3.0 27.0 1.0 C1A A:HEM182 3.0 25.8 1.0 C1C A:HEM182 3.1 26.6 1.0 C4B A:HEM182 3.1 25.3 1.0 C1D A:HEM182 3.1 27.9 1.0 C4C A:HEM182 3.1 27.2 1.0 C1B A:HEM182 3.1 25.3 1.0 C4A A:HEM182 3.1 25.6 1.0 CHA A:HEM182 3.4 26.1 1.0 CHC A:HEM182 3.4 26.2 1.0 CHD A:HEM182 3.5 27.4 1.0 CHB A:HEM182 3.5 25.7 1.0 NB B:HEM183 3.6 24.6 1.0 C4B B:HEM183 3.6 25.3 1.0 CHC B:HEM183 3.7 25.5 1.0 CGA B:HEM181 3.8 36.3 1.0 C1C B:HEM183 3.9 26.9 1.0 NC B:HEM183 3.9 26.8 1.0 FE B:HEM183 4.1 26.4 1.0 CBA B:HEM181 4.3 31.9 1.0 C3D A:HEM182 4.3 27.9 1.0 CE B:MET66 4.3 19.6 1.0 C2A A:HEM182 4.3 26.4 1.0 C2C A:HEM182 4.3 28.0 1.0 C2D A:HEM182 4.3 28.1 1.0 C3B A:HEM182 4.3 25.4 1.0 C3C A:HEM182 4.3 28.4 1.0 C2B A:HEM182 4.3 25.3 1.0 C1B B:HEM183 4.3 24.7 1.0 C3A A:HEM182 4.3 24.7 1.0 C3B B:HEM183 4.4 25.3 1.0 C2B B:HEM183 4.8 24.8 1.0 C2C B:HEM183 4.8 27.2 1.0 C4C B:HEM183 4.8 27.3 1.0 O2A B:HEM181 4.8 39.7 1.0 NA B:HEM183 5.0 24.7 1.0

Iron binding site 2 out of 4 in the Crystal Structure of the Cell Surface Heme Transfer Protein Shp


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 Cell Surface Heme Transfer Protein Shp within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe184 b:22.0 occ:1.00 FE A:HEM184 0.0 22.0 1.0 NB A:HEM184 2.0 20.3 1.0 NA A:HEM184 2.1 22.0 1.0 ND A:HEM184 2.1 21.9 1.0 NC A:HEM184 2.1 21.1 1.0 SD A:MET153 2.4 19.4 1.0 SD A:MET66 2.4 24.1 1.0 C4B A:HEM184 3.0 20.8 1.0 C1A A:HEM184 3.1 23.0 1.0 C4D A:HEM184 3.1 23.8 1.0 C1B A:HEM184 3.1 20.8 1.0 C1C A:HEM184 3.1 21.0 1.0 C1D A:HEM184 3.1 23.0 1.0 C4C A:HEM184 3.1 21.8 1.0 C4A A:HEM184 3.1 22.9 1.0 CG A:MET153 3.4 19.6 1.0 CE A:MET66 3.4 22.2 1.0 CHA A:HEM184 3.4 22.7 1.0 CHC A:HEM184 3.4 20.7 1.0 CE A:MET153 3.4 17.6 1.0 CHD A:HEM184 3.4 22.1 1.0 CHB A:HEM184 3.5 21.4 1.0 CG A:MET66 3.5 21.7 1.0 CB A:MET66 4.1 21.4 1.0 C3B A:HEM184 4.3 20.9 1.0 C2B A:HEM184 4.3 20.6 1.0 C2A A:HEM184 4.3 23.2 1.0 C3C A:HEM184 4.3 21.5 1.0 C3D A:HEM184 4.3 24.2 1.0 C2C A:HEM184 4.3 20.7 1.0 C3A A:HEM184 4.3 22.3 1.0 C2D A:HEM184 4.3 23.9 1.0 CB A:MET153 4.8 20.8 1.0

Iron binding site 3 out of 4 in the Crystal Structure of the Cell Surface Heme Transfer Protein Shp


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of the Cell Surface Heme Transfer Protein Shp within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe181 b:22.2 occ:1.00 FE B:HEM181 0.0 22.2 1.0 NA B:HEM181 2.0 21.1 1.0 NC B:HEM181 2.1 20.9 1.0 NB B:HEM181 2.1 21.0 1.0 ND B:HEM181 2.1 20.5 1.0 SD B:MET66 2.4 20.7 1.0 SD B:MET153 2.4 20.9 1.0 C1A B:HEM181 3.0 23.3 1.0 C4C B:HEM181 3.1 21.6 1.0 C4A B:HEM181 3.1 22.9 1.0 C4D B:HEM181 3.1 21.1 1.0 C1B B:HEM181 3.1 21.2 1.0 C1D B:HEM181 3.1 21.4 1.0 C4B B:HEM181 3.1 21.6 1.0 C1C B:HEM181 3.1 20.7 1.0 CE B:MET66 3.4 19.6 1.0 CG B:MET66 3.4 20.6 1.0 CHA B:HEM181 3.4 21.1 1.0 CG B:MET153 3.4 22.3 1.0 CHB B:HEM181 3.4 22.2 1.0 CHD B:HEM181 3.4 21.1 1.0 CHC B:HEM181 3.5 21.3 1.0 CE B:MET153 3.5 21.1 1.0 CB B:MET66 4.0 21.1 1.0 C2A B:HEM181 4.3 24.1 1.0 C3A B:HEM181 4.3 22.7 1.0 C3C B:HEM181 4.3 21.3 1.0 C2B B:HEM181 4.3 21.5 1.0 C3B B:HEM181 4.3 21.1 1.0 C3D B:HEM181 4.3 22.3 1.0 C2C B:HEM181 4.3 19.5 1.0 C2D B:HEM181 4.3 21.9 1.0 CB B:MET153 4.8 21.9 1.0 CG1 B:VAL150 5.0 20.7 1.0

Iron binding site 4 out of 4 in the Crystal Structure of the Cell Surface Heme Transfer Protein Shp


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of the Cell Surface Heme Transfer Protein Shp within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe183 b:26.4 occ:1.00 FE B:HEM183 0.0 26.4 1.0 NA B:HEM183 2.0 24.7 1.0 NB B:HEM183 2.0 24.6 1.0 NC B:HEM183 2.1 26.8 1.0 ND B:HEM183 2.1 26.8 1.0 O2D A:HEM184 2.9 41.7 1.0 C1A B:HEM183 3.0 24.8 1.0 C1C B:HEM183 3.1 26.9 1.0 C4A B:HEM183 3.1 24.8 1.0 C1B B:HEM183 3.1 24.7 1.0 C4B B:HEM183 3.1 25.3 1.0 C4D B:HEM183 3.1 26.9 1.0 C4C B:HEM183 3.1 27.3 1.0 C1D B:HEM183 3.1 28.1 1.0 CHA B:HEM183 3.4 24.9 1.0 CHC B:HEM183 3.4 25.5 1.0 CHB B:HEM183 3.4 24.7 1.0 CHD B:HEM183 3.5 27.6 1.0 C4B A:HEM182 3.6 25.3 1.0 NB A:HEM182 3.7 24.6 1.0 CHC A:HEM182 3.7 26.2 1.0 CGD A:HEM184 3.8 39.5 1.0 C1C A:HEM182 3.9 26.6 1.0 NC A:HEM182 3.9 26.5 1.0 FE A:HEM182 4.1 27.1 1.0 C2A B:HEM183 4.3 24.9 1.0 C3A B:HEM183 4.3 24.2 1.0 CE A:MET66 4.3 22.2 1.0 C2C B:HEM183 4.3 27.2 1.0 C2B B:HEM183 4.3 24.8 1.0 C3B B:HEM183 4.3 25.3 1.0 C3C B:HEM183 4.3 27.3 1.0 C1B A:HEM182 4.3 25.3 1.0 C3D B:HEM183 4.3 28.6 1.0 C3B A:HEM182 4.4 25.4 1.0 C2D B:HEM183 4.4 28.8 1.0 CBD A:HEM184 4.4 35.0 1.0 C2B A:HEM182 4.7 25.3 1.0 O1D A:HEM184 4.7 43.3 1.0 CD1 A:ILE62 4.8 30.6 1.0 C4C A:HEM182 4.8 27.2 1.0 C2C A:HEM182 4.8 28.0 1.0 NA A:HEM182 5.0 26.1 1.0

R.Aranda Iv, C.E.Worley, M.Liu, E.Bitto, M.S.Cates, J.S.Olson, B.Lei, G.N.Phillips Jr.. Bis-Methionyl Coordination in the Crystal Structure of the Heme-Binding Domain of the Streptococcal Cell Surface Protein Shp. J.Mol.Biol. V. 374 374 2007.
ISSN: ISSN 0022-2836
PubMed: 17920629
DOI: 10.1016/J.JMB.2007.08.058