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Copper in PDB 1rjo: Agao + Xe

Enzymatic activity of Agao + Xe

All present enzymatic activity of Agao + Xe:
1.4.3.6;

Protein crystallography data

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

Resolution Low / High (Å) 26.30 / 1.67
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 158.009, 63.189, 92.149, 90.00, 112.09, 90.00
R / Rfree (%) 15.7 / 17.8

Other elements in 1rjo:

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

Xenon (Xe) 7 atoms
Sodium (Na) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Agao + Xe (pdb code 1rjo). 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 Agao + Xe, PDB code: 1rjo:

Copper binding site 1 out of 1 in 1rjo

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


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Agao + Xe within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:23.7
occ:1.00
NE2 A:HIS433 2.0 15.6 1.0
ND1 A:HIS592 2.0 19.4 1.0
NE2 A:HIS431 2.1 14.4 1.0
O A:HOH1745 2.8 29.1 1.0
CD2 A:HIS431 3.0 13.8 1.0
CG A:HIS592 3.0 14.7 1.0
CD2 A:HIS433 3.0 16.6 1.0
CE1 A:HIS433 3.0 17.4 1.0
CE1 A:HIS592 3.0 16.6 1.0
CE1 A:HIS431 3.0 14.4 1.0
CB A:HIS592 3.3 13.9 1.0
O A:HOH1550 3.5 40.0 1.0
ND1 A:HIS433 4.1 15.0 1.0
ND1 A:HIS431 4.1 12.3 1.0
CG A:HIS431 4.1 12.9 1.0
NE2 A:HIS592 4.1 15.9 1.0
CD2 A:HIS592 4.2 15.7 1.0
CG A:HIS433 4.2 13.7 1.0
O A:HOH1208 4.5 23.1 1.0
CA A:HIS592 4.8 14.4 1.0
SD A:MET602 4.9 31.3 1.0
O A:HOH1551 4.9 37.2 1.0
O2 A:TPQ382 4.9 28.5 1.0

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 11:01:38 2020

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