Copper in PDB 5b80: Crystal Structure of Hyperthermophilic Thermotoga Maritima L-Ketose-3- Epimerase with CU2+

The structure of Crystal Structure of Hyperthermophilic Thermotoga Maritima L-Ketose-3- Epimerase with CU2+, PDB code: 5b80 was solved by T.P.Cao, S.M.Shin, D.W.Lee, S.H.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.25 / 1.70
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	50.282, 55.252, 58.763, 107.04, 102.49, 91.80
R / Rfree (%)	16.6 / 19

The binding sites of Copper atom in the Crystal Structure of Hyperthermophilic Thermotoga Maritima L-Ketose-3- Epimerase with CU2+ (pdb code 5b80). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Hyperthermophilic Thermotoga Maritima L-Ketose-3- Epimerase with CU2+, PDB code: 5b80:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of Hyperthermophilic Thermotoga Maritima L-Ketose-3- Epimerase with CU2+


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Hyperthermophilic Thermotoga Maritima L-Ketose-3- Epimerase with CU2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu301 b:46.1 occ:1.00 ND1 A:HIS208 2.1 11.9 1.0 OE1 A:GLU243 2.2 28.2 0.5 OE2 A:GLU149 2.2 12.5 1.0 OD2 A:ASP182 2.2 11.6 1.0 CD A:GLU243 2.9 26.9 0.5 CE1 A:HIS208 2.9 12.5 1.0 OE2 A:GLU243 2.9 39.7 0.5 CG A:HIS208 3.1 11.8 1.0 CD A:GLU149 3.2 13.4 1.0 CG A:ASP182 3.3 10.1 1.0 OE1 A:GLU149 3.5 14.8 1.0 CB A:HIS208 3.5 7.6 1.0 CB A:ASP182 3.7 7.7 1.0 CG A:GLU243 3.8 17.7 0.5 NH2 A:ARG214 4.0 14.2 0.5 O A:HOH465 4.0 11.9 1.0 NE2 A:HIS208 4.1 11.9 1.0 CD2 A:HIS208 4.2 10.7 1.0 CG A:GLU243 4.2 17.7 0.5 O A:HOH574 4.3 30.6 1.0 OD1 A:ASP182 4.4 10.5 1.0 CD2 A:HIS185 4.5 10.9 1.0 CB A:GLU243 4.5 12.3 0.5 CB A:GLU243 4.5 12.3 0.5 CG A:GLU149 4.6 5.8 1.0 NE2 A:HIS185 4.7 12.5 1.0 CD A:GLU243 4.9 26.9 0.5 CA A:ASP182 5.0 6.0 1.0

Copper binding site 2 out of 2 in the Crystal Structure of Hyperthermophilic Thermotoga Maritima L-Ketose-3- Epimerase with CU2+


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Hyperthermophilic Thermotoga Maritima L-Ketose-3- Epimerase with CU2+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu301 b:43.9 occ:1.00 OD2 B:ASP182 2.2 11.4 1.0 ND1 B:HIS208 2.2 14.5 1.0 OE2 B:GLU149 2.2 15.0 1.0 O B:HOH519 2.2 28.8 1.0 OE2 B:GLU243 2.4 32.7 0.5 CE1 B:HIS208 3.2 16.8 1.0 CG B:ASP182 3.2 9.3 1.0 CG B:HIS208 3.2 12.7 1.0 CD B:GLU149 3.2 15.5 1.0 O B:HOH408 3.3 32.0 1.0 CB B:HIS208 3.5 12.4 1.0 CD B:GLU243 3.5 31.7 0.5 CB B:ASP182 3.5 8.9 1.0 OE1 B:GLU149 3.6 16.4 1.0 O B:HOH442 4.0 15.5 1.0 OE1 B:GLU243 4.1 39.8 0.5 OE2 B:GLU243 4.2 32.7 0.5 NH2 B:ARG214 4.2 20.3 0.5 OD1 B:ASP182 4.2 11.8 1.0 CG B:GLU243 4.3 23.7 0.5 NE2 B:HIS208 4.3 17.0 1.0 CD2 B:HIS208 4.3 12.1 1.0 CD B:GLU243 4.3 31.7 0.5 CD2 B:HIS185 4.4 11.4 1.0 CB B:GLU243 4.5 15.3 0.5 CG B:GLU149 4.5 8.7 1.0 CB B:GLU243 4.6 15.3 0.5 CG B:GLU243 4.6 23.7 0.5 NE2 B:HIS185 4.7 13.1 1.0 O B:HOH503 4.8 26.5 1.0 CA B:ASP182 4.8 8.4 1.0

S.M.Shin, T.P.Cao, J.M.Choi, S.B.Kim, S.J.Lee, S.H.Lee, D.W.Lee. TM0416, A Hyperthermophilic Promiscuous Nonphosphorylated Sugar Isomerase, Catalyzes Various C5AND C6EPIMERIZATION Reactions Appl. Environ. Microbiol. V. 83 2017.
ISSN: ESSN 1098-5336
PubMed: 28258150
DOI: 10.1128/AEM.03291-16