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Copper in PDB 1rky: Pplo + Xe

Enzymatic activity of Pplo + Xe

All present enzymatic activity of Pplo + Xe:
1.4.3.13;

Protein crystallography data

The structure of Pplo + Xe, PDB code: 1rky was solved by J.M.Guss, A.P.Duff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.47 / 1.68
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 140.144, 66.702, 108.620, 90.00, 119.24, 90.00
R / Rfree (%) 15.1 / 18.2

Other elements in 1rky:

The structure of Pplo + Xe also contains other interesting chemical elements:

Magnesium (Mg) 3 atoms
Xenon (Xe) 8 atoms
Calcium (Ca) 2 atoms
Chlorine (Cl) 6 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Pplo + Xe (pdb code 1rky). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Pplo + Xe, PDB code: 1rky:

Copper binding site 1 out of 1 in 1rky

Go back to Copper Binding Sites List in 1rky
Copper binding site 1 out of 1 in the Pplo + Xe


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Pplo + Xe within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu801

b:32.4
occ:1.00
ND1 A:HIS694 2.0 28.0 1.0
NE2 A:HIS528 2.0 26.6 1.0
NE2 A:HIS530 2.1 31.0 1.0
O4 A:TPQ478 2.4 36.7 0.7
CE1 A:HIS694 2.9 30.8 1.0
CE1 A:HIS528 3.0 28.6 1.0
CD2 A:HIS528 3.0 27.5 1.0
CD2 A:HIS530 3.0 31.8 1.0
CE1 A:HIS530 3.0 31.7 1.0
CG A:HIS694 3.1 25.2 1.0
C4 A:TPQ478 3.1 52.4 0.7
CB A:HIS694 3.4 22.8 1.0
O5 A:TPQ478 3.6 73.7 0.7
C5 A:TPQ478 3.7 70.9 0.7
NE2 A:HIS694 4.1 26.3 1.0
C3 A:TPQ478 4.1 49.2 0.7
ND1 A:HIS528 4.1 26.7 1.0
CG A:HIS528 4.1 23.8 1.0
CD2 A:HIS694 4.1 28.3 1.0
ND1 A:HIS530 4.1 29.6 1.0
O A:HOH2003 4.2 32.9 1.0
CG A:HIS530 4.2 27.9 1.0
CD2 A:LEU692 4.9 32.9 1.0
CA A:HIS694 4.9 23.4 1.0
C6 A:TPQ478 5.0 65.8 0.7

Reference:

A.P.Duff, D.M.Trambaiolo, A.E.Cohen, P.J.Ellis, G.A.Juda, E.M.Shepard, D.B.Langley, D.M.Dooley, H.C.Freeman, J.M.Guss. Using Xenon As A Probe For Dioxygen-Binding Sites in Copper Amine Oxidases J.Mol.Biol. V. 344 599 2004.
ISSN: ISSN 0022-2836
PubMed: 15533431
DOI: 10.1016/J.JMB.2004.09.075
Page generated: Sun Dec 13 11:01:45 2020

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