Iron in PDB 4f30: Structure of RPE65: P6522 Crystal Form Grown in Ammonium Phosphate Solution

All present enzymatic activity of Structure of RPE65: P6522 Crystal Form Grown in Ammonium Phosphate Solution:
3.1.1.64;

The structure of Structure of RPE65: P6522 Crystal Form Grown in Ammonium Phosphate Solution, PDB code: 4f30 was solved by P.D.Kiser, K.Palczewski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.44 / 3.15
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	178.497, 178.497, 86.642, 90.00, 90.00, 120.00
R / Rfree (%)	21.5 / 24.7

The binding sites of Iron atom in the Structure of RPE65: P6522 Crystal Form Grown in Ammonium Phosphate Solution (pdb code 4f30). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Structure of RPE65: P6522 Crystal Form Grown in Ammonium Phosphate Solution, PDB code: 4f30:

Iron binding site 1 out of 1 in the Structure of RPE65: P6522 Crystal Form Grown in Ammonium Phosphate Solution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of RPE65: P6522 Crystal Form Grown in Ammonium Phosphate Solution within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:50.3 occ:1.00 NE2 A:HIS527 2.2 51.3 1.0 NE2 A:HIS180 2.2 48.7 1.0 NE2 A:HIS313 2.2 47.1 1.0 NE2 A:HIS241 2.2 54.0 1.0 CD2 A:HIS241 3.0 51.5 1.0 CE1 A:HIS527 3.0 49.3 1.0 CD2 A:HIS313 3.1 46.1 1.0 CE1 A:HIS180 3.1 48.5 1.0 CD2 A:HIS180 3.1 49.0 1.0 CD2 A:HIS527 3.2 51.8 1.0 CE1 A:HIS313 3.2 46.6 1.0 CE1 A:HIS241 3.3 54.6 1.0 ND1 A:HIS527 4.1 49.1 1.0 CG A:HIS241 4.2 50.5 1.0 CG A:HIS527 4.2 50.6 1.0 CG A:HIS313 4.3 45.2 1.0 ND1 A:HIS180 4.3 49.0 1.0 ND1 A:HIS241 4.3 52.8 1.0 ND1 A:HIS313 4.3 44.9 1.0 CG A:HIS180 4.3 48.4 1.0 CG1 A:VAL134 4.8 49.4 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