Iron in PDB 1aa6: Reduced Form of Formate Dehydrogenase H From E. Coli

All present enzymatic activity of Reduced Form of Formate Dehydrogenase H From E. Coli:
1.2.1.2;

The structure of Reduced Form of Formate Dehydrogenase H From E. Coli, PDB code: 1aa6 was solved by P.D.Sun, J.C.Boyington, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 2.30
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	146.400, 146.400, 82.700, 90.00, 90.00, 90.00
R / Rfree (%)	21.7 / 28.7

The structure of Reduced Form of Formate Dehydrogenase H From E. Coli also contains other interesting chemical elements:

Molybdenum

(Mo)

1 atom

The binding sites of Iron atom in the Reduced Form of Formate Dehydrogenase H From E. Coli (pdb code 1aa6). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Reduced Form of Formate Dehydrogenase H From E. Coli, PDB code: 1aa6:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Reduced Form of Formate Dehydrogenase H From E. Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Reduced Form of Formate Dehydrogenase H From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe800 b:19.6 occ:1.00 FE1 A:SF4800 0.0 19.6 1.0 SG A:CYS42 2.3 15.1 1.0 S2 A:SF4800 2.3 17.3 1.0 S3 A:SF4800 2.3 15.7 1.0 S4 A:SF4800 2.3 16.4 1.0 FE2 A:SF4800 2.7 17.9 1.0 FE4 A:SF4800 2.7 17.0 1.0 FE3 A:SF4800 2.8 19.3 1.0 CB A:CYS42 3.3 19.3 1.0 N A:CYS42 3.8 19.8 1.0 S1 A:SF4800 3.9 16.3 1.0 CA A:CYS42 4.1 20.1 1.0 N A:GLY45 4.4 19.1 1.0 CD A:PRO182 4.5 14.6 1.0 C A:CYS42 4.5 20.9 1.0 CG A:PRO182 4.6 13.8 1.0 O A:CYS42 4.6 21.6 1.0 NZ A:LYS44 4.6 28.1 1.0 CE A:LYS44 4.6 26.6 1.0 CB A:PRO182 4.7 13.0 1.0 CB A:LYS44 4.7 20.5 1.0 SG A:CYS8 4.8 18.6 1.0 O A:HOH833 4.8 22.3 1.0 SG A:CYS11 4.8 13.9 1.0 SG A:CYS15 4.9 17.0 1.0 N A:LYS44 4.9 21.2 1.0 C A:LEU41 5.0 20.5 1.0

Iron binding site 2 out of 4 in the Reduced Form of Formate Dehydrogenase H From E. Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Reduced Form of Formate Dehydrogenase H From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe800 b:17.9 occ:1.00 FE2 A:SF4800 0.0 17.9 1.0 S1 A:SF4800 2.2 16.3 1.0 SG A:CYS8 2.3 18.6 1.0 S3 A:SF4800 2.3 15.7 1.0 S4 A:SF4800 2.4 16.4 1.0 FE3 A:SF4800 2.6 19.3 1.0 FE4 A:SF4800 2.7 17.0 1.0 FE1 A:SF4800 2.7 19.6 1.0 CB A:CYS8 3.1 16.5 1.0 S2 A:SF4800 3.8 17.3 1.0 CB A:TYR10 4.2 14.4 1.0 N A:GLY45 4.3 19.1 1.0 CA A:GLY45 4.3 20.4 1.0 CA A:CYS8 4.5 16.6 1.0 SG A:CYS15 4.6 17.0 1.0 N A:CYS11 4.6 12.6 1.0 CB A:CYS15 4.6 12.8 1.0 SG A:CYS42 4.7 15.1 1.0 CD2 A:TYR10 4.8 14.9 1.0 SG A:CYS11 4.9 13.9 1.0 N A:TYR10 4.9 12.9 1.0 O A:CYS11 4.9 11.1 1.0 CA A:TYR10 5.0 14.5 1.0

Iron binding site 3 out of 4 in the Reduced Form of Formate Dehydrogenase H From E. Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Reduced Form of Formate Dehydrogenase H From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe800 b:19.3 occ:1.00 FE3 A:SF4800 0.0 19.3 1.0 SG A:CYS15 2.2 17.0 1.0 S2 A:SF4800 2.3 17.3 1.0 S4 A:SF4800 2.3 16.4 1.0 S1 A:SF4800 2.3 16.3 1.0 FE2 A:SF4800 2.6 17.9 1.0 FE4 A:SF4800 2.8 17.0 1.0 FE1 A:SF4800 2.8 19.6 1.0 CB A:CYS15 3.2 12.8 1.0 S3 A:SF4800 4.0 15.7 1.0 CB A:SER13 4.0 10.4 1.0 N A:CYS15 4.3 15.2 1.0 CD1 A:ILE183 4.3 10.2 1.0 CA A:CYS15 4.3 14.8 1.0 CG1 A:ILE183 4.3 11.8 1.0 CB A:ILE183 4.4 12.4 1.0 CB A:CYS8 4.5 16.5 1.0 SG A:CYS8 4.6 18.6 1.0 OG A:SER13 4.6 12.1 1.0 N A:CYS42 4.8 19.8 1.0 SG A:CYS11 4.9 13.9 1.0 CD2 A:LEU41 4.9 20.0 1.0

Iron binding site 4 out of 4 in the Reduced Form of Formate Dehydrogenase H From E. Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Reduced Form of Formate Dehydrogenase H From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe800 b:17.0 occ:1.00 FE4 A:SF4800 0.0 17.0 1.0 S3 A:SF4800 2.3 15.7 1.0 S1 A:SF4800 2.3 16.3 1.0 S2 A:SF4800 2.3 17.3 1.0 SG A:CYS11 2.4 13.9 1.0 FE2 A:SF4800 2.7 17.9 1.0 FE1 A:SF4800 2.7 19.6 1.0 FE3 A:SF4800 2.8 19.3 1.0 CB A:CYS11 3.5 12.7 1.0 N A:CYS11 3.9 12.6 1.0 CB A:SER13 3.9 10.4 1.0 OG A:SER13 3.9 12.1 1.0 S4 A:SF4800 4.0 16.4 1.0 CA A:CYS11 4.0 12.7 1.0 O A:HOH833 4.0 22.3 1.0 O A:CYS11 4.0 11.1 1.0 C A:CYS11 4.2 12.4 1.0 N A:SER13 4.5 12.7 1.0 CD A:PRO182 4.6 14.6 1.0 SG A:CYS8 4.6 18.6 1.0 NZ A:LYS44 4.7 28.1 1.0 SG A:CYS42 4.7 15.1 1.0 SG A:CYS15 4.8 17.0 1.0 CA A:SER13 4.8 12.9 1.0 CB A:TYR10 4.8 14.4 1.0

J.C.Boyington, V.N.Gladyshev, S.V.Khangulov, T.C.Stadtman, P.D.Sun. Crystal Structure of Formate Dehydrogenase H: Catalysis Involving Mo, Molybdopterin, Selenocysteine, and An FE4S4 Cluster. Science V. 275 1305 1997.
ISSN: ISSN 0036-8075
PubMed: 9036855
DOI: 10.1126/SCIENCE.275.5304.1305