Iron in PDB 4f3d: Structure of RPE65: P65 Crystal Form Grown in Fos-Choline-10

All present enzymatic activity of Structure of RPE65: P65 Crystal Form Grown in Fos-Choline-10:
3.1.1.64;

The structure of Structure of RPE65: P65 Crystal Form Grown in Fos-Choline-10, PDB code: 4f3d 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)	47.80 / 2.50
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	175.258, 175.258, 86.449, 90.00, 90.00, 120.00
R / Rfree (%)	19.3 / 21.9

The binding sites of Iron atom in the Structure of RPE65: P65 Crystal Form Grown in Fos-Choline-10 (pdb code 4f3d). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of RPE65: P65 Crystal Form Grown in Fos-Choline-10, PDB code: 4f3d:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of RPE65: P65 Crystal Form Grown in Fos-Choline-10


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: P65 Crystal Form Grown in Fos-Choline-10 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:33.1 occ:1.00 NE2 A:HIS241 2.2 32.3 1.0 NE2 A:HIS527 2.3 29.7 1.0 NE2 A:HIS180 2.3 28.9 1.0 NE2 A:HIS313 2.4 32.2 1.0 CD2 A:HIS241 3.2 30.1 1.0 CE1 A:HIS527 3.2 30.2 1.0 CE1 A:HIS241 3.2 31.3 1.0 CD2 A:HIS313 3.2 32.2 1.0 CD2 A:HIS527 3.2 29.6 1.0 CE1 A:HIS180 3.2 29.1 1.0 CD2 A:HIS180 3.4 28.6 1.0 CE1 A:HIS313 3.5 30.5 1.0 ND1 A:HIS527 4.3 30.3 1.0 ND1 A:HIS241 4.3 32.9 1.0 CG A:HIS241 4.3 31.1 1.0 CG A:HIS527 4.3 30.4 1.0 ND1 A:HIS180 4.4 29.2 1.0 CG A:HIS313 4.4 31.2 1.0 CG A:HIS180 4.5 28.8 1.0 ND1 A:HIS313 4.5 32.9 1.0 CG1 A:VAL134 4.8 38.0 1.0 O A:HOH714 4.9 40.2 1.0 CE2 A:PHE418 5.0 38.8 1.0

Iron binding site 2 out of 2 in the Structure of RPE65: P65 Crystal Form Grown in Fos-Choline-10


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of RPE65: P65 Crystal Form Grown in Fos-Choline-10 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:37.7 occ:1.00 NE2 B:HIS241 2.2 35.3 1.0 NE2 B:HIS527 2.3 31.0 1.0 NE2 B:HIS313 2.3 35.9 1.0 NE2 B:HIS180 2.3 33.6 1.0 CD2 B:HIS313 3.1 35.2 1.0 CD2 B:HIS241 3.1 33.7 1.0 CE1 B:HIS527 3.2 31.2 1.0 CE1 B:HIS241 3.2 35.4 1.0 CE1 B:HIS180 3.2 32.5 1.0 CD2 B:HIS527 3.3 31.9 1.0 CD2 B:HIS180 3.4 31.6 1.0 CE1 B:HIS313 3.4 35.2 1.0 ND1 B:HIS527 4.3 31.4 1.0 ND1 B:HIS241 4.3 35.8 1.0 CG B:HIS241 4.3 33.7 1.0 CG B:HIS313 4.4 34.5 1.0 CG B:HIS527 4.4 32.5 1.0 ND1 B:HIS180 4.4 33.7 1.0 ND1 B:HIS313 4.4 36.7 1.0 CG B:HIS180 4.5 32.1 1.0 CG1 B:VAL134 4.8 39.0 1.0 O B:HOH708 4.9 41.7 1.0 CE2 B:PHE418 5.0 36.9 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