Atomistry » Copper » PDB 2aps-2cg1 » 2hx8
Atomistry »
  Copper »
    PDB 2aps-2cg1 »
      2hx8 »

Copper in PDB 2hx8: Crystal Structure of Cu(I) Azurin with the Metal-Binding Loop Sequence "Ctfpghsalm" Replaced with "Csphqgagm", at PH5

Protein crystallography data

The structure of Crystal Structure of Cu(I) Azurin with the Metal-Binding Loop Sequence "Ctfpghsalm" Replaced with "Csphqgagm", at PH5, PDB code: 2hx8 was solved by M.J.Banfield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 54.31 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 38.905, 65.345, 97.707, 90.00, 90.00, 90.00
R / Rfree (%) 13.8 / 18.4

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Cu(I) Azurin with the Metal-Binding Loop Sequence "Ctfpghsalm" Replaced with "Csphqgagm", at PH5 (pdb code 2hx8). 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 Cu(I) Azurin with the Metal-Binding Loop Sequence "Ctfpghsalm" Replaced with "Csphqgagm", at PH5, PDB code: 2hx8:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2hx8

Go back to Copper Binding Sites List in 2hx8
Copper binding site 1 out of 2 in the Crystal Structure of Cu(I) Azurin with the Metal-Binding Loop Sequence "Ctfpghsalm" Replaced with "Csphqgagm", at PH5


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 Cu(I) Azurin with the Metal-Binding Loop Sequence "Ctfpghsalm" Replaced with "Csphqgagm", at PH5 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:13.2
occ:1.00
ND1 A:HIS46 2.0 9.1 1.0
ND1 A:HIS115 2.1 13.1 1.0
SG A:CYS112 2.2 10.2 1.0
CE1 A:HIS46 3.0 10.0 1.0
CE1 A:HIS115 3.1 12.9 1.0
CG A:HIS46 3.1 8.9 1.0
CG A:HIS115 3.1 12.0 1.0
SD A:MET120 3.1 13.2 1.0
O A:GLY45 3.2 9.9 1.0
CB A:CYS112 3.2 9.5 1.0
CB A:HIS115 3.4 11.3 1.0
CA A:HIS46 3.4 9.3 1.0
CB A:HIS46 3.5 9.8 1.0
CE A:MET120 3.8 13.1 1.0
C A:GLY45 4.0 9.9 1.0
NE2 A:HIS46 4.1 10.2 1.0
N A:HIS46 4.1 8.8 1.0
CD2 A:HIS46 4.2 10.6 1.0
NE2 A:HIS115 4.2 11.3 1.0
CD2 A:HIS115 4.2 13.5 1.0
CG A:PRO114 4.2 11.3 1.0
N A:HIS115 4.3 10.0 1.0
CA A:HIS115 4.5 10.7 1.0
CG A:MET120 4.5 14.9 1.0
C A:HIS46 4.6 9.2 1.0
N A:ASN47 4.6 9.1 1.0
CA A:CYS112 4.7 8.8 1.0
CD A:PRO114 4.9 10.5 1.0
CB A:MET120 4.9 12.5 1.0

Copper binding site 2 out of 2 in 2hx8

Go back to Copper Binding Sites List in 2hx8
Copper binding site 2 out of 2 in the Crystal Structure of Cu(I) Azurin with the Metal-Binding Loop Sequence "Ctfpghsalm" Replaced with "Csphqgagm", at PH5


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 Cu(I) Azurin with the Metal-Binding Loop Sequence "Ctfpghsalm" Replaced with "Csphqgagm", at PH5 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu201

b:12.1
occ:1.00
ND1 B:HIS46 2.1 9.5 1.0
ND1 B:HIS115 2.1 11.6 1.0
SG B:CYS112 2.2 9.1 1.0
CE1 B:HIS46 3.0 8.2 1.0
CG B:HIS115 3.1 8.9 1.0
CE1 B:HIS115 3.1 9.2 1.0
CG B:HIS46 3.1 8.5 1.0
SD B:MET120 3.1 9.7 1.0
CB B:CYS112 3.3 8.4 1.0
O B:GLY45 3.3 9.6 1.0
CB B:HIS115 3.3 8.8 1.0
CA B:HIS46 3.4 9.3 1.0
CB B:HIS46 3.5 9.3 1.0
CE B:MET120 3.7 11.4 1.0
C B:GLY45 4.1 9.8 1.0
CG B:PRO114 4.1 9.4 1.0
NE2 B:HIS46 4.1 9.9 1.0
N B:HIS46 4.2 9.2 1.0
NE2 B:HIS115 4.2 9.8 1.0
CD2 B:HIS115 4.2 10.9 1.0
CD2 B:HIS46 4.2 9.7 1.0
N B:HIS115 4.2 8.9 1.0
CA B:HIS115 4.4 8.5 1.0
C B:HIS46 4.6 8.7 1.0
CG B:MET120 4.6 8.9 1.0
N B:ASN47 4.6 7.8 1.0
CA B:CYS112 4.7 7.2 1.0
CD B:PRO114 4.8 10.3 1.0
CB B:MET120 4.8 9.4 1.0
CB B:PRO114 5.0 9.5 1.0

Reference:

C.Li, M.J.Banfield, C.Dennison. Engineering Copper Sites in Proteins: Loops Confer Native Structures and Properties to Chimeric Cupredoxins. J.Am.Chem.Soc. V. 129 709 2007.
ISSN: ISSN 0002-7863
PubMed: 17227035
DOI: 10.1021/JA0661562
Page generated: Thu Sep 3 16:41:47 2020
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy