Atomistry » Copper » PDB 1oe2-1rjp » 1oxy
Atomistry »
  Copper »
    PDB 1oe2-1rjp »
      1oxy »

Copper in PDB 1oxy: Crystallographic Analysis of Oxygenated and Deoxygenated States of Arthropod Hemocyanin Shows Unusual Differences

Protein crystallography data

The structure of Crystallographic Analysis of Oxygenated and Deoxygenated States of Arthropod Hemocyanin Shows Unusual Differences, PDB code: 1oxy was solved by H.Ton-That, K.Magnus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.40
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 117.240, 117.240, 285.860, 90.00, 90.00, 120.00
R / Rfree (%) 17.1 / n/a

Copper Binding Sites:

The binding sites of Copper atom in the Crystallographic Analysis of Oxygenated and Deoxygenated States of Arthropod Hemocyanin Shows Unusual Differences (pdb code 1oxy). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystallographic Analysis of Oxygenated and Deoxygenated States of Arthropod Hemocyanin Shows Unusual Differences, PDB code: 1oxy:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1oxy

Go back to Copper Binding Sites List in 1oxy
Copper binding site 1 out of 2 in the Crystallographic Analysis of Oxygenated and Deoxygenated States of Arthropod Hemocyanin Shows Unusual Differences


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystallographic Analysis of Oxygenated and Deoxygenated States of Arthropod Hemocyanin Shows Unusual Differences within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu629

b:20.0
occ:1.00
NE2 A:HIS324 1.9 12.3 1.0
O2 A:OXY631 2.1 24.8 1.0
NE2 A:HIS364 2.1 11.6 1.0
O1 A:OXY631 2.2 26.5 1.0
NE2 A:HIS328 2.4 21.5 1.0
CE1 A:HIS364 2.5 8.8 1.0
CE1 A:HIS324 2.7 10.7 1.0
CD2 A:HIS324 3.0 7.6 1.0
CD2 A:HIS328 3.2 16.6 1.0
CD2 A:HIS364 3.3 17.0 1.0
CE1 A:HIS328 3.5 16.9 1.0
CU A:CU630 3.6 22.6 1.0
ND1 A:HIS364 3.8 17.3 1.0
ND1 A:HIS324 3.8 13.1 1.0
CG A:HIS324 4.0 10.4 1.0
CD2 A:HIS204 4.0 11.0 1.0
NE2 A:HIS204 4.1 11.4 1.0
CE2 A:PHE360 4.1 14.4 1.0
CG A:HIS364 4.2 14.2 1.0
CE1 A:PHE49 4.3 10.0 1.0
CG A:HIS328 4.4 13.8 1.0
CZ A:PHE360 4.5 12.7 1.0
ND1 A:HIS328 4.5 19.1 1.0
CZ A:PHE49 4.7 15.1 1.0
CD2 A:PHE360 4.9 10.9 1.0
CE1 A:PHE200 4.9 17.6 1.0

Copper binding site 2 out of 2 in 1oxy

Go back to Copper Binding Sites List in 1oxy
Copper binding site 2 out of 2 in the Crystallographic Analysis of Oxygenated and Deoxygenated States of Arthropod Hemocyanin Shows Unusual Differences


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystallographic Analysis of Oxygenated and Deoxygenated States of Arthropod Hemocyanin Shows Unusual Differences within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu630

b:22.6
occ:1.00
O2 A:OXY631 1.7 24.8 1.0
O1 A:OXY631 2.0 26.5 1.0
NE2 A:HIS177 2.1 12.3 1.0
NE2 A:HIS173 2.2 13.8 1.0
NE2 A:HIS204 2.4 11.4 1.0
CE1 A:HIS177 2.9 13.1 1.0
CD2 A:HIS177 3.1 9.8 1.0
CD2 A:HIS173 3.1 16.3 1.0
CE1 A:HIS173 3.2 16.3 1.0
CD2 A:HIS204 3.3 11.0 1.0
CE1 A:HIS204 3.4 14.6 1.0
CU A:CU629 3.6 20.0 1.0
ND1 A:HIS177 4.1 12.9 1.0
CG A:HIS177 4.2 15.1 1.0
ND1 A:HIS173 4.3 18.6 1.0
CG A:HIS173 4.3 17.1 1.0
CG A:HIS204 4.4 13.1 1.0
ND1 A:HIS204 4.5 15.0 1.0
CE2 A:PHE360 4.7 14.4 1.0
CG2 A:THR351 4.7 22.0 1.0
CZ A:PHE360 4.7 12.7 1.0
NE2 A:HIS324 4.8 12.3 1.0
CZ A:PHE49 4.8 15.1 1.0
NE2 A:HIS364 4.8 11.6 1.0
CE1 A:HIS324 4.8 10.7 1.0
CE1 A:PHE49 4.9 10.0 1.0

Reference:

K.A.Magnus, B.Hazes, H.Ton-That, C.Bonaventura, J.Bonaventura, W.G.Hol. Crystallographic Analysis of Oxygenated and Deoxygenated States of Arthropod Hemocyanin Shows Unusual Differences. Proteins V. 19 302 1994.
ISSN: ISSN 0887-3585
PubMed: 7984626
DOI: 10.1002/PROT.340190405
Page generated: Tue Jul 30 22:33:34 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy