Iron in PDB 3aeu: Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark

The structure of Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark, PDB code: 3aeu was solved by N.Muraki, J.Nomata, T.Shiba, Y.Fujita, G.Kurisu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.90 / 2.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	81.354, 80.615, 176.220, 90.00, 101.17, 90.00
R / Rfree (%)	20.5 / 25.7

The binding sites of Iron atom in the Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark (pdb code 3aeu). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark, PDB code: 3aeu:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in the Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe425 b:18.7 occ:1.00 FE1 A:SF4425 0.0 18.7 1.0 S4 A:SF4425 2.3 22.6 1.0 S3 A:SF4425 2.3 21.6 1.0 S2 A:SF4425 2.3 19.5 1.0 SG A:CYS26 2.5 15.9 1.0 FE2 A:SF4425 2.7 27.9 1.0 FE4 A:SF4425 2.7 14.7 1.0 FE3 A:SF4425 2.8 18.9 1.0 CB A:CYS26 3.3 16.2 1.0 CD2 A:LEU28 3.9 12.8 1.0 S1 A:SF4425 4.0 22.2 1.0 N A:GLY145 4.2 18.4 1.0 CD2 A:LEU54 4.6 12.2 1.0 CA A:GLY145 4.7 18.1 1.0 CG A:LEU28 4.7 12.3 1.0 CB A:LEU28 4.8 13.4 1.0 CA A:CYS26 4.8 16.2 1.0 SG A:CYS112 4.9 21.2 1.0 CD1 A:LEU28 4.9 11.4 1.0

Iron binding site 2 out of 8 in the Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe425 b:27.9 occ:1.00 FE2 A:SF4425 0.0 27.9 1.0 S1 A:SF4425 2.3 22.2 1.0 S4 A:SF4425 2.3 22.6 1.0 S3 A:SF4425 2.3 21.6 1.0 FE4 A:SF4425 2.6 14.7 1.0 FE3 A:SF4425 2.7 18.9 1.0 FE1 A:SF4425 2.7 18.7 1.0 S2 A:SF4425 3.8 19.5 1.0 CG2 A:THR50 4.0 15.8 1.0 CG B:PRO33 4.5 16.7 1.0 SG A:CYS112 4.8 21.2 1.0 CB A:THR50 4.8 17.1 1.0 SG A:CYS51 4.9 16.1 1.0 N B:ALA36 5.0 19.4 1.0 SG A:CYS26 5.0 15.9 1.0 C B:GLY35 5.0 19.1 1.0

Iron binding site 3 out of 8 in the Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe425 b:18.9 occ:1.00 FE3 A:SF4425 0.0 18.9 1.0 S2 A:SF4425 2.3 19.5 1.0 S4 A:SF4425 2.3 22.6 1.0 S1 A:SF4425 2.3 22.2 1.0 SG A:CYS51 2.5 16.1 1.0 FE2 A:SF4425 2.7 27.9 1.0 FE4 A:SF4425 2.7 14.7 1.0 FE1 A:SF4425 2.8 18.7 1.0 CB A:CYS51 3.6 16.5 1.0 CD2 A:LEU28 3.8 12.8 1.0 CA A:CYS51 3.9 16.7 1.0 S3 A:SF4425 3.9 21.6 1.0 N A:CYS51 4.2 16.8 1.0 CB A:SER111 4.2 18.3 1.0 CD A:PRO113 4.4 20.2 1.0 N A:CYS112 4.6 19.1 1.0 SG A:CYS112 4.9 21.2 1.0 C A:THR50 5.0 16.9 1.0

Iron binding site 4 out of 8 in the Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe425 b:14.7 occ:1.00 FE4 A:SF4425 0.0 14.7 1.0 S1 A:SF4425 2.3 22.2 1.0 S2 A:SF4425 2.3 19.5 1.0 S3 A:SF4425 2.3 21.6 1.0 SG A:CYS112 2.4 21.2 1.0 FE2 A:SF4425 2.6 27.9 1.0 FE3 A:SF4425 2.7 18.9 1.0 FE1 A:SF4425 2.7 18.7 1.0 CB A:CYS112 3.2 19.9 1.0 N A:GLY145 3.7 18.4 1.0 N A:CYS112 3.8 19.1 1.0 S4 A:SF4425 3.9 22.6 1.0 CA A:CYS112 4.1 19.9 1.0 CG B:PRO33 4.2 16.7 1.0 CA A:GLY145 4.3 18.1 1.0 CD A:PRO113 4.4 20.2 1.0 OG1 B:THR96 4.5 28.2 1.0 CB B:PRO33 4.6 16.6 1.0 CA A:SER144 4.7 18.9 1.0 C A:SER144 4.7 18.6 1.0 CB A:SER144 4.8 18.9 1.0 C A:SER111 4.9 18.6 1.0 SG A:CYS26 5.0 15.9 1.0

Iron binding site 5 out of 8 in the Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe425 b:19.3 occ:1.00 FE1 C:SF4425 0.0 19.3 1.0 S4 C:SF4425 2.3 21.0 1.0 S3 C:SF4425 2.3 17.8 1.0 S2 C:SF4425 2.3 18.9 1.0 SG C:CYS26 2.5 16.3 1.0 FE2 C:SF4425 2.7 29.7 1.0 FE4 C:SF4425 2.7 19.7 1.0 FE3 C:SF4425 2.7 17.9 1.0 CB C:CYS26 3.5 16.3 1.0 CD2 C:LEU28 3.8 11.2 1.0 S1 C:SF4425 3.9 21.9 1.0 CD2 C:LEU54 4.0 14.6 1.0 N C:GLY145 4.2 18.3 1.0 CA C:GLY145 4.7 18.1 1.0 SG C:CYS51 4.8 19.0 1.0 CG C:LEU28 4.9 12.9 1.0 CB C:LEU28 4.9 13.3 1.0 SG C:CYS112 4.9 20.3 1.0 CA C:CYS26 4.9 16.2 1.0

Iron binding site 6 out of 8 in the Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe425 b:29.7 occ:1.00 FE2 C:SF4425 0.0 29.7 1.0 S3 C:SF4425 2.3 17.8 1.0 S1 C:SF4425 2.3 21.9 1.0 S4 C:SF4425 2.3 21.0 1.0 FE4 C:SF4425 2.7 19.7 1.0 FE1 C:SF4425 2.7 19.3 1.0 FE3 C:SF4425 2.7 17.9 1.0 S2 C:SF4425 3.9 18.9 1.0 CG2 C:THR50 4.1 17.2 1.0 CG D:PRO33 4.2 16.2 1.0 SG C:CYS112 4.7 20.3 1.0 C D:GLY35 4.7 18.9 1.0 O D:GLY35 4.8 18.4 1.0 N D:ALA36 4.8 19.4 1.0 CA D:ALA36 4.9 20.0 1.0 SG C:CYS51 4.9 19.0 1.0 SG C:CYS26 5.0 16.3 1.0 CG2 D:THR96 5.0 28.3 1.0

Iron binding site 7 out of 8 in the Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe425 b:17.9 occ:1.00 FE3 C:SF4425 0.0 17.9 1.0 S4 C:SF4425 2.3 21.0 1.0 S2 C:SF4425 2.3 18.9 1.0 S1 C:SF4425 2.3 21.9 1.0 SG C:CYS51 2.4 19.0 1.0 FE1 C:SF4425 2.7 19.3 1.0 FE2 C:SF4425 2.7 29.7 1.0 FE4 C:SF4425 2.7 19.7 1.0 CB C:CYS51 3.6 17.5 1.0 CD2 C:LEU28 3.9 11.2 1.0 CA C:CYS51 3.9 17.0 1.0 S3 C:SF4425 3.9 17.8 1.0 N C:CYS51 4.2 16.8 1.0 CD C:PRO113 4.3 20.1 1.0 CB C:SER111 4.3 18.2 1.0 N C:CYS112 4.7 19.0 1.0 CG2 C:THR50 4.9 17.2 1.0 C C:THR50 4.9 17.1 1.0 SG C:CYS112 4.9 20.3 1.0 CG C:PRO113 5.0 20.0 1.0

Iron binding site 8 out of 8 in the Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe425 b:19.7 occ:1.00 FE4 C:SF4425 0.0 19.7 1.0 S1 C:SF4425 2.3 21.9 1.0 S2 C:SF4425 2.3 18.9 1.0 S3 C:SF4425 2.3 17.8 1.0 SG C:CYS112 2.4 20.3 1.0 FE2 C:SF4425 2.7 29.7 1.0 FE1 C:SF4425 2.7 19.3 1.0 FE3 C:SF4425 2.7 17.9 1.0 CB C:CYS112 3.2 19.5 1.0 N C:GLY145 3.5 18.3 1.0 N C:CYS112 3.7 19.0 1.0 S4 C:SF4425 3.9 21.0 1.0 CA C:CYS112 4.0 19.6 1.0 CA C:GLY145 4.1 18.1 1.0 CG D:PRO33 4.2 16.2 1.0 CD C:PRO113 4.5 20.1 1.0 CA C:SER144 4.5 19.0 1.0 C C:SER144 4.5 18.6 1.0 CG2 D:THR96 4.6 28.3 1.0 CB C:SER144 4.7 19.3 1.0 CB D:PRO33 4.8 17.1 1.0 C C:SER111 4.8 18.7 1.0 SG C:CYS26 4.8 16.3 1.0 SG C:CYS51 4.8 19.0 1.0

N.Muraki, J.Nomata, K.Ebata, T.Mizoguchi, T.Shiba, H.Tamiaki, G.Kurisu, Y.Fujita. X-Ray Crystal Structure of the Light-Independent Protochlorophyllide Reductase Nature V. 465 110 2010.
ISSN: ISSN 0028-0836
PubMed: 20400946
DOI: 10.1038/NATURE08950