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Copper in PDB 2hxa: Crystal Structure of Cu(I) Azurin with the Metal-Binding Loop Sequence "Ctfpghsalm" Replaced with "Csphqgagm", at PH3.5

Protein crystallography data

The structure of Crystal Structure of Cu(I) Azurin with the Metal-Binding Loop Sequence "Ctfpghsalm" Replaced with "Csphqgagm", at PH3.5, PDB code: 2hxa 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) 35.56 / 2.21
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 38.338, 65.726, 97.577, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 26.7

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 PH3.5 (pdb code 2hxa). 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 PH3.5, PDB code: 2hxa:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2hxa

Go back to Copper Binding Sites List in 2hxa
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 PH3.5


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 PH3.5 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:26.2
occ:1.00
ND1 A:HIS46 2.2 17.2 1.0
SG A:CYS112 2.2 15.6 1.0
ND1 A:HIS115 2.4 20.6 1.0
CE1 A:HIS46 3.0 16.0 1.0
O A:GLY45 3.2 17.6 1.0
CG A:HIS46 3.2 16.8 1.0
SD A:MET120 3.2 18.6 1.0
CG A:HIS115 3.2 18.8 1.0
CB A:CYS112 3.2 15.4 1.0
CB A:HIS115 3.3 18.6 1.0
CA A:HIS46 3.4 16.7 1.0
CE1 A:HIS115 3.4 20.0 1.0
CB A:HIS46 3.6 16.5 1.0
CE A:MET120 3.8 16.8 1.0
C A:GLY45 4.0 17.6 1.0
N A:HIS46 4.1 17.6 1.0
NE2 A:HIS46 4.2 16.6 1.0
N A:HIS115 4.2 18.1 1.0
CD2 A:HIS46 4.2 16.9 1.0
CA A:HIS115 4.4 18.4 1.0
CG A:PRO114 4.4 17.9 1.0
CD2 A:HIS115 4.4 20.2 1.0
N A:ASN47 4.5 16.0 1.0
NE2 A:HIS115 4.5 19.5 1.0
C A:HIS46 4.5 16.3 1.0
CA A:CYS112 4.7 15.5 1.0
CG A:MET120 4.7 18.6 1.0
CD A:PRO114 4.9 16.8 1.0
CB A:MET120 5.0 18.8 1.0

Copper binding site 2 out of 2 in 2hxa

Go back to Copper Binding Sites List in 2hxa
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 PH3.5


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 PH3.5 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu201

b:19.1
occ:1.00
SG B:CYS112 2.1 14.4 1.0
ND1 B:HIS46 2.2 14.3 1.0
ND1 B:HIS115 2.2 14.8 1.0
CG B:HIS115 3.1 14.7 1.0
CE1 B:HIS46 3.1 12.7 1.0
CG B:HIS46 3.2 14.4 1.0
O B:GLY45 3.2 15.8 1.0
CE1 B:HIS115 3.3 14.9 1.0
CB B:HIS115 3.3 13.6 1.0
SD B:MET120 3.3 13.2 1.0
CB B:CYS112 3.4 13.9 1.0
CA B:HIS46 3.4 14.1 1.0
CB B:HIS46 3.5 14.3 1.0
CE B:MET120 3.8 8.8 1.0
C B:GLY45 4.1 15.7 1.0
CG B:PRO114 4.1 14.7 1.0
N B:HIS46 4.2 14.7 1.0
N B:HIS115 4.2 14.1 1.0
NE2 B:HIS46 4.3 13.9 1.0
CD2 B:HIS115 4.3 12.9 1.0
CD2 B:HIS46 4.3 14.6 1.0
NE2 B:HIS115 4.3 12.9 1.0
CA B:HIS115 4.3 14.1 1.0
N B:ASN47 4.5 13.3 1.0
C B:HIS46 4.5 13.7 1.0
CA B:CYS112 4.7 14.3 1.0
CD B:PRO114 4.8 14.2 1.0
CG B:MET120 4.8 11.2 1.0
CB B:PRO114 4.8 14.8 1.0
CB B:MET120 5.0 12.3 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: Sun Dec 13 11:05:13 2020

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