Cobalt in PDB 4djf: Crystal Structure of Folate-Bound Corrinoid Iron-Sulfur Protein (Cfesp) in Complex with Its Methyltransferase (Metr), Co-Crystallized with Folate and Ti(III) Citrate Reductant

The structure of Crystal Structure of Folate-Bound Corrinoid Iron-Sulfur Protein (Cfesp) in Complex with Its Methyltransferase (Metr), Co-Crystallized with Folate and Ti(III) Citrate Reductant, PDB code: 4djf was solved by Y.Kung, C.L.Drennan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.75 / 3.03
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	136.006, 250.686, 81.800, 90.00, 90.00, 90.00
R / Rfree (%)	26.9 / 30.8

The structure of Crystal Structure of Folate-Bound Corrinoid Iron-Sulfur Protein (Cfesp) in Complex with Its Methyltransferase (Metr), Co-Crystallized with Folate and Ti(III) Citrate Reductant also contains other interesting chemical elements:

Iron	(Fe)	8 atoms
Calcium	(Ca)	2 atoms

The binding sites of Cobalt atom in the Crystal Structure of Folate-Bound Corrinoid Iron-Sulfur Protein (Cfesp) in Complex with Its Methyltransferase (Metr), Co-Crystallized with Folate and Ti(III) Citrate Reductant (pdb code 4djf). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Crystal Structure of Folate-Bound Corrinoid Iron-Sulfur Protein (Cfesp) in Complex with Its Methyltransferase (Metr), Co-Crystallized with Folate and Ti(III) Citrate Reductant, PDB code: 4djf:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Crystal Structure of Folate-Bound Corrinoid Iron-Sulfur Protein (Cfesp) in Complex with Its Methyltransferase (Metr), Co-Crystallized with Folate and Ti(III) Citrate Reductant


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of Folate-Bound Corrinoid Iron-Sulfur Protein (Cfesp) in Complex with Its Methyltransferase (Metr), Co-Crystallized with Folate and Ti(III) Citrate Reductant within 5.0Å range: probe atom residue distance (Å) B Occ C:Co502 b:0.7 occ:1.00 CO C:COB502 0.0 0.7 1.0 N23 C:COB502 1.8 0.7 1.0 N21 C:COB502 1.8 0.7 1.0 N24 C:COB502 1.9 0.7 1.0 N22 C:COB502 1.9 0.7 1.0 C1A C:COB502 2.0 0.7 1.0 C11 C:COB502 2.8 0.7 1.0 C9 C:COB502 2.8 0.7 1.0 C4 C:COB502 2.9 0.7 1.0 C19 C:COB502 2.9 0.7 1.0 C14 C:COB502 2.9 0.7 1.0 C1 C:COB502 2.9 0.7 1.0 C16 C:COB502 2.9 0.7 1.0 C6 C:COB502 3.0 0.7 1.0 C10 C:COB502 3.2 0.7 1.0 C5 C:COB502 3.3 0.7 1.0 C15 C:COB502 3.4 0.7 1.0 OG1 C:THR375 3.4 94.8 1.0 C20 C:COB502 3.6 0.7 1.0 CG2 C:THR375 3.9 94.8 1.0 CB C:THR375 4.1 94.8 1.0 C2 C:COB502 4.1 0.7 1.0 C13 C:COB502 4.1 0.7 1.0 C18 C:COB502 4.1 0.7 1.0 C12 C:COB502 4.1 0.7 1.0 C3 C:COB502 4.2 0.7 1.0 C17 C:COB502 4.2 0.7 1.0 C8 C:COB502 4.2 0.7 1.0 C7 C:COB502 4.3 0.7 1.0 C26 C:COB502 4.4 0.7 1.0 CA C:THR375 4.6 0.3 1.0 C48 C:COB502 4.6 0.7 1.0 C46 C:COB502 4.7 0.7 1.0 C54 C:COB502 4.7 0.7 1.0 C37 C:COB502 4.9 0.7 1.0 C35 C:COB502 4.9 0.7 1.0 C53 C:COB502 4.9 0.7 1.0 C41 C:COB502 5.0 0.7 1.0

Cobalt binding site 2 out of 2 in the Crystal Structure of Folate-Bound Corrinoid Iron-Sulfur Protein (Cfesp) in Complex with Its Methyltransferase (Metr), Co-Crystallized with Folate and Ti(III) Citrate Reductant


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Crystal Structure of Folate-Bound Corrinoid Iron-Sulfur Protein (Cfesp) in Complex with Its Methyltransferase (Metr), Co-Crystallized with Folate and Ti(III) Citrate Reductant within 5.0Å range: probe atom residue distance (Å) B Occ E:Co502 b:0.7 occ:1.00 CO E:COB502 0.0 0.7 1.0 N23 E:COB502 1.8 0.7 1.0 N21 E:COB502 1.8 0.7 1.0 N24 E:COB502 1.9 0.7 1.0 N22 E:COB502 1.9 0.7 1.0 C1A E:COB502 1.9 0.7 1.0 C11 E:COB502 2.8 0.7 1.0 C9 E:COB502 2.8 0.7 1.0 C4 E:COB502 2.9 0.7 1.0 C1 E:COB502 2.9 0.7 1.0 C19 E:COB502 2.9 0.7 1.0 C14 E:COB502 2.9 0.7 1.0 C16 E:COB502 2.9 0.7 1.0 OG1 E:THR375 3.0 97.2 1.0 C6 E:COB502 3.0 0.7 1.0 C10 E:COB502 3.2 0.7 1.0 C5 E:COB502 3.3 0.7 1.0 C15 E:COB502 3.4 0.7 1.0 C20 E:COB502 3.6 0.7 1.0 CB E:THR375 4.1 97.2 1.0 C2 E:COB502 4.1 0.7 1.0 C18 E:COB502 4.1 0.7 1.0 C12 E:COB502 4.1 0.7 1.0 C13 E:COB502 4.2 0.7 1.0 C3 E:COB502 4.2 0.7 1.0 C17 E:COB502 4.2 0.7 1.0 C8 E:COB502 4.2 0.7 1.0 C7 E:COB502 4.3 0.7 1.0 CG2 E:THR375 4.3 97.2 1.0 C26 E:COB502 4.5 0.7 1.0 CA E:THR375 4.6 0.3 1.0 C46 E:COB502 4.7 0.7 1.0 C54 E:COB502 4.8 0.7 1.0 C48 E:COB502 4.8 0.7 1.0 C35 E:COB502 4.9 0.7 1.0 C37 E:COB502 4.9 0.7 1.0 CG2 A:VAL168 4.9 94.3 1.0 C53 E:COB502 4.9 0.7 1.0 C41 E:COB502 5.0 0.7 1.0

Y.Kung, N.Ando, T.I.Doukov, L.C.Blasiak, G.Bender, J.Seravalli, S.W.Ragsdale, C.L.Drennan. Visualizing Molecular Juggling Within A B12-Dependent Methyltransferase Complex. Nature V. 484 265 2012.
ISSN: ISSN 0028-0836
PubMed: 22419154
DOI: 10.1038/NATURE10916