Cobalt in PDB 7nyt: Trichoderma Reesei CEL7A E212Q Mutant in Complex with Lactose.

All present enzymatic activity of Trichoderma Reesei CEL7A E212Q Mutant in Complex with Lactose.:
3.2.1.91;

The structure of Trichoderma Reesei CEL7A E212Q Mutant in Complex with Lactose., PDB code: 7nyt was solved by T.Haataja, M.Sandgren, J.Stahlberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.77 / 1.09
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	83.54, 82.21, 110.734, 90, 90, 90
R / Rfree (%)	12.3 / 14.3

The binding sites of Cobalt atom in the Trichoderma Reesei CEL7A E212Q Mutant in Complex with Lactose. (pdb code 7nyt). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Trichoderma Reesei CEL7A E212Q Mutant in Complex with Lactose., PDB code: 7nyt:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Trichoderma Reesei CEL7A E212Q Mutant in Complex with Lactose.


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Trichoderma Reesei CEL7A E212Q Mutant in Complex with Lactose. within 5.0Å range: probe atom residue distance (Å) B Occ A:Co505 b:6.6 occ:0.50 OE2 A:GLU325 2.1 7.5 1.0 OE1 A:GLU295 2.2 7.1 1.0 OE2 A:GLU295 2.2 7.5 1.0 CD A:GLU295 2.5 6.7 1.0 CD A:GLU325 3.1 7.3 1.0 OE1 A:GLU325 3.5 7.8 1.0 O A:HOH757 3.9 10.7 1.0 ND2 A:ASN301 4.0 8.2 1.0 CG A:GLU295 4.0 7.3 1.0 O A:HOH722 4.3 9.4 1.0 CG A:GLU325 4.4 6.9 1.0 OG A:SER297 4.8 8.2 1.0 CB A:ALA299 4.8 6.8 1.0 CB A:GLU295 4.9 7.8 1.0 O A:HOH981 4.9 8.9 1.0

Cobalt binding site 2 out of 2 in the Trichoderma Reesei CEL7A E212Q Mutant in Complex with Lactose.


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Trichoderma Reesei CEL7A E212Q Mutant in Complex with Lactose. within 5.0Å range: probe atom residue distance (Å) B Occ A:Co506 b:35.3 occ:1.00 O A:HOH710 1.7 42.0 1.0 NE2 A:HIS206 1.8 17.9 0.5 O A:HOH619 1.8 49.6 1.0 OE2 A:GLU239 1.9 35.2 1.0 O A:HOH795 2.0 33.3 1.0 NE2 A:HIS206 2.2 13.7 0.5 CE1 A:HIS206 2.6 16.8 0.5 CD A:GLU239 2.9 24.4 1.0 CD2 A:HIS206 2.9 16.4 0.5 CD2 A:HIS206 3.2 14.0 0.5 CE1 A:HIS206 3.2 14.0 0.5 OE1 A:GLU239 3.2 34.4 1.0 ND1 A:HIS206 3.7 15.6 0.5 CG A:HIS206 3.9 14.2 0.5 CG A:GLU239 4.3 21.1 1.0 ND1 A:HIS206 4.3 12.9 0.5 CG A:HIS206 4.3 12.7 0.5 O A:HOH641 4.3 20.4 0.5 O A:HOH675 4.6 28.3 1.0

T.Haataja, J.E.Gado, A.Nutt, N.T.Anderson, M.Nilsson, M.H.Momeni, R.Isaksson, P.Valjamae, G.Johansson, C.M.Payne, J.Stahlberg. Enzyme Kinetics By GH7 Cellobiohydrolases on Chromogenic Substrates Is Dictated By Non-Productive Binding: Insights From Crystal Structures and Md Simulation. Febs J. 2022.
ISSN: ISSN 1742-464X
PubMed: 35997626
DOI: 10.1111/FEBS.16602