Atomistry » Copper » PDB 3awt-3erx » 3e0i
Atomistry »
  Copper »
    PDB 3awt-3erx »
      3e0i »

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

Enzymatic activity of 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;

Protein crystallography data

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

Copper Binding Sites:

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 3e0i

Go back to Copper Binding Sites List in 3e0i
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 3e0i

Go back to Copper Binding Sites List in 3e0i
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

Reference:

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
Page generated: Sun Dec 13 11:09:25 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy