Copper in PDB 3e0i: CU2+ Substituted Aquifex Aeolicus KDO8PS in Complex with Pep

All present enzymatic activity of CU2+ Substituted Aquifex Aeolicus KDO8PS in Complex with Pep:
2.5.1.55;

The structure of CU2+ Substituted Aquifex Aeolicus KDO8PS in Complex with Pep, PDB code: 3e0i was solved by D.L.Gatti, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	21.20 / 1.70
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	84.789, 84.789, 159.902, 90.00, 90.00, 120.00
R / Rfree (%)	13.5 / 16.6

The binding sites of Copper atom in the CU2+ Substituted Aquifex Aeolicus KDO8PS in Complex with Pep (pdb code 3e0i). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the CU2+ Substituted Aquifex Aeolicus KDO8PS in Complex with Pep, PDB code: 3e0i:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the CU2+ Substituted Aquifex Aeolicus KDO8PS in Complex with Pep


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of CU2+ Substituted Aquifex Aeolicus KDO8PS in Complex with Pep within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu3270 b:18.5 occ:0.79 NE2 A:HIS1185 2.1 17.6 1.0 OE1 A:GLU1222 2.2 20.5 1.0 SG A:CYS1011 2.3 21.0 1.0 OE2 A:GLU1222 2.6 22.0 1.0 CD A:GLU1222 2.7 20.8 1.0 OD2 A:ASP1233 2.9 35.8 1.0 CE1 A:HIS1185 2.9 18.5 1.0 O A:HOH5196 3.0 28.8 1.0 CD2 A:HIS1185 3.2 20.5 1.0 CB A:CYS1011 3.3 16.8 1.0 CG A:ASP1233 3.7 31.6 1.0 O A:HOH5480 4.0 32.6 1.0 NZ A:LYS1046 4.0 19.5 1.0 CB A:ASP1233 4.1 23.9 1.0 CA A:CYS1011 4.1 15.9 1.0 ND1 A:HIS1185 4.1 17.3 1.0 O1 A:PEP3268 4.2 17.7 1.0 CG A:GLU1222 4.2 18.2 1.0 CG A:HIS1185 4.3 15.9 1.0 C1 A:PEP3268 4.3 14.9 1.0 NZ A:LYS1041 4.3 14.2 1.0 O2' A:PEP3268 4.6 15.1 1.0 OD1 A:ASP1233 4.6 39.4 1.0 CE A:LYS1046 4.8 16.5 1.0 O A:HOH5583 4.8 33.2 1.0 C A:CYS1011 4.8 15.8 1.0 C2 A:PEP3268 4.9 16.4 1.0 CB A:GLU1222 5.0 15.6 1.0 O A:CYS1011 5.0 16.4 1.0

Copper binding site 2 out of 2 in the CU2+ Substituted Aquifex Aeolicus KDO8PS in Complex with Pep


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of CU2+ Substituted Aquifex Aeolicus KDO8PS in Complex with Pep within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu4270 b:19.9 occ:0.80 NE2 B:HIS2185 2.1 20.0 1.0 SG B:CYS2011 2.3 22.2 1.0 OE1 B:GLU2222 2.3 25.8 1.0 OD2 B:ASP2233 2.5 38.4 1.0 OE2 B:GLU2222 2.6 23.6 1.0 CD B:GLU2222 2.8 23.3 1.0 CE1 B:HIS2185 2.9 20.2 1.0 O B:HOH5186 3.1 31.9 1.0 CD2 B:HIS2185 3.2 20.9 1.0 CB B:CYS2011 3.3 19.4 1.0 CG B:ASP2233 3.6 32.9 1.0 NZ B:LYS2046 4.0 19.1 1.0 ND1 B:HIS2185 4.1 18.2 1.0 CB B:ASP2233 4.1 27.2 1.0 CA B:CYS2011 4.1 18.2 1.0 O1 B:PEP4268 4.1 19.4 1.0 O B:HOH5423 4.2 35.9 1.0 CG B:GLU2222 4.2 21.2 1.0 CG B:HIS2185 4.3 18.0 1.0 NZ B:LYS2041 4.3 15.5 1.0 C1 B:PEP4268 4.3 18.9 1.0 O2' B:PEP4268 4.6 17.7 1.0 OD1 B:ASP2233 4.6 38.6 1.0 CE B:LYS2046 4.8 17.7 1.0 C2 B:PEP4268 4.9 17.1 1.0 NE2 B:GLN2188 4.9 37.3 0.5 C B:CYS2011 4.9 18.3 1.0 CB B:GLU2222 5.0 18.1 1.0 O B:HOH5286 5.0 34.2 1.0 O B:CYS2011 5.0 19.1 1.0

F.Kona, P.Tao, P.Martin, X.Xu, D.L.Gatti. Electronic Structure of the Metal Center in the Cd(2+), Zn(2+), and Cu(2+) Substituted Forms of KDO8P Synthase: Implications For Catalysis. Biochemistry V. 48 3610 2009.
ISSN: ISSN 0006-2960
PubMed: 19228070
DOI: 10.1021/BI801955H