Iron in PDB 4f2z: Crystal Structure of RPE65 in A Lipid Environment

All present enzymatic activity of Crystal Structure of RPE65 in A Lipid Environment:
3.1.1.64;

The structure of Crystal Structure of RPE65 in A Lipid Environment, PDB code: 4f2z was solved by P.D.Kiser, W.Shi, K.Palczewski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	69.40 / 3.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.799, 100.234, 277.588, 90.00, 90.00, 90.00
R / Rfree (%)	22.4 / 26.1

The binding sites of Iron atom in the Crystal Structure of RPE65 in A Lipid Environment (pdb code 4f2z). 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 RPE65 in A Lipid Environment, PDB code: 4f2z:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of RPE65 in A Lipid Environment


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 RPE65 in A Lipid Environment within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:58.9 occ:1.00 NE2 A:HIS241 2.1 64.5 1.0 NE2 A:HIS180 2.2 60.8 1.0 NE2 A:HIS313 2.2 50.9 1.0 NE2 A:HIS527 2.2 60.0 1.0 CE1 A:HIS241 3.1 66.8 1.0 CD2 A:HIS527 3.1 59.3 1.0 CE1 A:HIS527 3.1 57.0 1.0 CD2 A:HIS241 3.1 63.0 1.0 CE1 A:HIS313 3.1 49.6 1.0 CD2 A:HIS180 3.1 61.2 1.0 CE1 A:HIS180 3.1 62.2 1.0 CD2 A:HIS313 3.2 49.9 1.0 ND1 A:HIS527 4.2 57.2 1.0 CG A:HIS527 4.2 58.1 1.0 ND1 A:HIS241 4.2 66.7 1.0 CG A:HIS241 4.2 63.2 1.0 ND1 A:HIS313 4.3 49.5 1.0 ND1 A:HIS180 4.3 62.2 1.0 CG A:HIS180 4.3 59.3 1.0 CG A:HIS313 4.3 49.4 1.0 CG1 A:VAL134 4.6 57.5 1.0

Iron binding site 2 out of 2 in the Crystal Structure of RPE65 in A Lipid Environment


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 RPE65 in A Lipid Environment within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe601 b:61.5 occ:1.00 NE2 E:HIS241 2.1 63.0 1.0 NE2 E:HIS313 2.2 56.9 1.0 NE2 E:HIS180 2.2 61.8 1.0 NE2 E:HIS527 2.2 61.2 1.0 CE1 E:HIS313 3.1 58.2 1.0 CD2 E:HIS527 3.1 59.5 1.0 CD2 E:HIS241 3.1 61.8 1.0 CE1 E:HIS527 3.1 58.0 1.0 CE1 E:HIS241 3.1 63.1 1.0 CD2 E:HIS180 3.1 61.1 1.0 CD2 E:HIS313 3.2 56.9 1.0 CE1 E:HIS180 3.2 60.8 1.0 ND1 E:HIS527 4.2 57.9 1.0 CG E:HIS527 4.2 59.1 1.0 ND1 E:HIS241 4.2 61.6 1.0 ND1 E:HIS313 4.2 57.8 1.0 CG E:HIS241 4.3 60.8 1.0 ND1 E:HIS180 4.3 59.2 1.0 CG E:HIS313 4.3 56.8 1.0 CG E:HIS180 4.3 58.9 1.0 CG1 E:VAL134 4.6 62.3 1.0

P.D.Kiser, E.R.Farquhar, W.Shi, X.Sui, M.R.Chance, K.Palczewski. Structure of RPE65 Isomerase in A Lipidic Matrix Reveals Roles For Phospholipids and Iron in Catalysis. Proc.Natl.Acad.Sci.Usa V. 109 E2747 2012.
ISSN: ISSN 0027-8424
PubMed: 23012475
DOI: 10.1073/PNAS.1212025109