Iron in PDB 3sel: Ppca M58N Mutant

The structure of Ppca M58N Mutant, PDB code: 3sel was solved by P.R.Pokkuluri, M.Schiffer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.10
Space group	P 43 2 2
Cell size a, b, c (Å), α, β, γ (°)	32.420, 32.420, 177.450, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 22.3

The binding sites of Iron atom in the Ppca M58N Mutant (pdb code 3sel). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Ppca M58N Mutant, PDB code: 3sel:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Ppca M58N Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Ppca M58N Mutant within 5.0Å range: probe atom residue distance (Å) B Occ X:Fe72 b:10.4 occ:1.00 FE X:HEM72 0.0 10.4 1.0 NC X:HEM72 2.0 10.0 1.0 NA X:HEM72 2.0 12.3 1.0 ND X:HEM72 2.0 12.6 1.0 NE2 X:HIS31 2.0 9.7 1.0 NB X:HEM72 2.0 10.2 1.0 NE2 X:HIS17 2.0 11.2 1.0 CD2 X:HIS17 2.9 10.9 1.0 C4C X:HEM72 3.0 11.7 1.0 CE1 X:HIS31 3.0 13.8 1.0 C4A X:HEM72 3.0 13.0 1.0 C1D X:HEM72 3.0 9.5 1.0 C1C X:HEM72 3.0 10.8 1.0 C1B X:HEM72 3.0 12.6 1.0 C1A X:HEM72 3.0 14.7 1.0 CD2 X:HIS31 3.1 12.1 1.0 C4D X:HEM72 3.1 11.2 1.0 C4B X:HEM72 3.1 11.5 1.0 CE1 X:HIS17 3.1 14.4 1.0 CHD X:HEM72 3.3 9.7 1.0 CHB X:HEM72 3.4 10.8 1.0 CHA X:HEM72 3.4 11.3 1.0 CHC X:HEM72 3.4 10.4 1.0 CG X:HIS17 4.1 11.8 1.0 ND1 X:HIS31 4.1 12.2 1.0 ND1 X:HIS17 4.1 13.2 1.0 CG X:HIS31 4.2 13.8 1.0 C3C X:HEM72 4.2 9.6 1.0 C2C X:HEM72 4.2 10.2 1.0 C3A X:HEM72 4.2 16.9 1.0 C2D X:HEM72 4.2 11.8 1.0 C2A X:HEM72 4.2 20.4 1.0 C3D X:HEM72 4.3 12.2 1.0 C2B X:HEM72 4.3 11.6 1.0 C3B X:HEM72 4.3 10.3 1.0 O1A X:HEM72 4.7 35.0 0.5

Iron binding site 2 out of 3 in the Ppca M58N Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Ppca M58N Mutant within 5.0Å range: probe atom residue distance (Å) B Occ X:Fe73 b:11.9 occ:1.00 FE X:HEM73 0.0 11.9 1.0 NE2 X:HIS55 2.0 13.6 1.0 NB X:HEM73 2.0 12.0 1.0 NE2 X:HIS20 2.0 11.1 1.0 ND X:HEM73 2.0 13.4 1.0 NA X:HEM73 2.1 13.5 1.0 NC X:HEM73 2.1 11.2 1.0 CE1 X:HIS55 2.9 11.8 1.0 CD2 X:HIS20 3.0 12.4 1.0 C1A X:HEM73 3.0 16.0 1.0 C4D X:HEM73 3.0 17.3 1.0 CD2 X:HIS55 3.0 12.6 1.0 C4B X:HEM73 3.0 12.2 1.0 CE1 X:HIS20 3.0 12.5 1.0 C1B X:HEM73 3.1 13.2 1.0 C1D X:HEM73 3.1 15.7 1.0 C1C X:HEM73 3.1 10.9 1.0 C4A X:HEM73 3.1 14.1 1.0 C4C X:HEM73 3.1 11.3 1.0 CHA X:HEM73 3.4 16.3 1.0 CHC X:HEM73 3.4 12.6 1.0 CHD X:HEM73 3.4 13.9 1.0 CHB X:HEM73 3.5 13.7 1.0 ND1 X:HIS55 4.0 12.9 1.0 ND1 X:HIS20 4.1 9.2 1.0 CG X:HIS20 4.1 11.1 1.0 CG X:HIS55 4.1 15.9 1.0 C2A X:HEM73 4.2 17.1 1.0 C3B X:HEM73 4.3 11.2 1.0 C2B X:HEM73 4.3 12.7 1.0 C3D X:HEM73 4.3 20.4 1.0 C3A X:HEM73 4.3 15.5 1.0 C2D X:HEM73 4.3 18.7 1.0 C3C X:HEM73 4.3 13.5 1.0 C2C X:HEM73 4.3 11.6 1.0

Iron binding site 3 out of 3 in the Ppca M58N Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Ppca M58N Mutant within 5.0Å range: probe atom residue distance (Å) B Occ X:Fe74 b:10.2 occ:1.00 FE X:HEM74 0.0 10.2 1.0 NE2 X:HIS47 1.9 9.7 1.0 NC X:HEM74 2.0 11.9 1.0 NB X:HEM74 2.0 10.7 1.0 ND X:HEM74 2.0 11.5 1.0 NE2 X:HIS69 2.1 10.6 1.0 NA X:HEM74 2.1 14.1 1.0 CE1 X:HIS47 2.9 13.5 1.0 CD2 X:HIS47 3.0 13.2 1.0 C1C X:HEM74 3.0 11.9 1.0 CE1 X:HIS69 3.0 10.3 1.0 C4C X:HEM74 3.0 12.4 1.0 C4B X:HEM74 3.0 11.7 1.0 C1B X:HEM74 3.0 9.3 1.0 C1D X:HEM74 3.0 12.5 1.0 C4D X:HEM74 3.1 15.5 1.0 C4A X:HEM74 3.1 13.0 1.0 CD2 X:HIS69 3.1 12.4 1.0 C1A X:HEM74 3.1 14.4 1.0 CHC X:HEM74 3.4 12.5 1.0 CHD X:HEM74 3.4 11.5 1.0 CHB X:HEM74 3.4 8.6 1.0 CHA X:HEM74 3.5 15.4 1.0 ND1 X:HIS47 4.0 11.5 1.0 CG X:HIS47 4.1 14.4 1.0 ND1 X:HIS69 4.1 10.2 1.0 CG X:HIS69 4.2 12.0 1.0 C2C X:HEM74 4.2 10.7 1.0 C3C X:HEM74 4.2 12.5 1.0 C2B X:HEM74 4.2 12.1 1.0 C3B X:HEM74 4.2 12.1 1.0 C2D X:HEM74 4.3 11.9 1.0 C3D X:HEM74 4.3 15.4 1.0 C3A X:HEM74 4.3 14.3 1.0 C2A X:HEM74 4.3 13.6 1.0 ND2 X:ASN10 4.5 8.3 1.0

P.R.Pokkuluri, X.Yang, Y.Y.Londer, M.Schiffer. Pitfalls in the Interpretation of Structural Changes in Mutant Proteins From Crystal Structures. J.Struct.Funct.Genom. V. 13 227 2012.
ISSN: ISSN 1345-711X
PubMed: 23099666
DOI: 10.1007/S10969-012-9147-1