Cobalt in PDB 2fua: L-Fuculose 1-Phosphate Aldolase Crystal Form T with Cobalt

All present enzymatic activity of L-Fuculose 1-Phosphate Aldolase Crystal Form T with Cobalt:
4.1.2.17;

The structure of L-Fuculose 1-Phosphate Aldolase Crystal Form T with Cobalt, PDB code: 2fua was solved by M.K.Dreyer, G.E.Schulz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.00
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	93.700, 93.700, 42.800, 90.00, 90.00, 90.00
R / Rfree (%)	18 / n/a

The binding sites of Cobalt atom in the L-Fuculose 1-Phosphate Aldolase Crystal Form T with Cobalt (pdb code 2fua). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the L-Fuculose 1-Phosphate Aldolase Crystal Form T with Cobalt, PDB code: 2fua:

Cobalt binding site 1 out of 1 in the L-Fuculose 1-Phosphate Aldolase Crystal Form T with Cobalt


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of L-Fuculose 1-Phosphate Aldolase Crystal Form T with Cobalt within 5.0Å range: probe atom residue distance (Å) B Occ A:Co216 b:6.5 occ:1.00 NE2 A:HIS94 1.9 11.1 1.0 NE2 A:HIS155 2.0 4.7 1.0 NE2 A:HIS92 2.1 7.2 1.0 OE2 A:GLU73 2.2 14.6 1.0 OE1 A:GLU73 2.3 9.9 1.0 CD A:GLU73 2.6 10.5 1.0 CE1 A:HIS94 2.8 13.3 1.0 CE1 A:HIS155 3.0 9.1 1.0 CE1 A:HIS92 3.0 2.0 1.0 CD2 A:HIS155 3.0 7.5 1.0 CD2 A:HIS94 3.1 9.8 1.0 CD2 A:HIS92 3.2 6.0 1.0 ND1 A:HIS94 4.0 13.6 1.0 CG A:GLU73 4.1 10.8 1.0 ND1 A:HIS155 4.1 4.6 1.0 O A:HOH449 4.1 23.6 1.0 CG A:HIS94 4.2 8.9 1.0 CG A:HIS155 4.2 3.5 1.0 ND1 A:HIS92 4.2 3.2 1.0 CG A:HIS92 4.3 4.3 1.0 CZ A:PHE76 4.5 4.5 1.0 O A:HOH475 4.7 42.9 1.0 O A:ALA27 4.7 38.2 1.0 CE2 A:PHE76 4.8 2.9 1.0 CB A:GLU73 4.9 10.2 1.0

M.K.Dreyer, G.E.Schulz. Refined High-Resolution Structure of the Metal-Ion Dependent L-Fuculose-1-Phosphate Aldolase (Class II) From Escherichia Coli. Acta Crystallogr.,Sect.D V. 52 1082 1996.
ISSN: ISSN 0907-4449
PubMed: 15299567
DOI: 10.1107/S0907444996009146