Atomistry » Copper » PDB 1tmx-1x9l » 1w4n
Atomistry »
  Copper »
    PDB 1tmx-1x9l »
      1w4n »

Copper in PDB 1w4n: Agao Covalent Complex with Tranylcypromine

Enzymatic activity of Agao Covalent Complex with Tranylcypromine

All present enzymatic activity of Agao Covalent Complex with Tranylcypromine:
1.4.3.6;

Protein crystallography data

The structure of Agao Covalent Complex with Tranylcypromine, PDB code: 1w4n was solved by A.P.Duff, D.M.Trambaiolo, D.B.Langley, G.A.Juda, E.M.Shepard, D.M.Dooley, H.C.Freeman, J.M.Guss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.28 / 1.65
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 158.113, 63.001, 184.490, 90.00, 112.04, 90.00
R / Rfree (%) 17.1 / 19.9

Other elements in 1w4n:

The structure of Agao Covalent Complex with Tranylcypromine also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Agao Covalent Complex with Tranylcypromine (pdb code 1w4n). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Agao Covalent Complex with Tranylcypromine, PDB code: 1w4n:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1w4n

Go back to Copper Binding Sites List in 1w4n
Copper binding site 1 out of 2 in the Agao Covalent Complex with Tranylcypromine


Mono view


Stereo pair view

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

b:29.1
occ:1.00
NE2 A:HIS431 2.0 10.2 1.0
ND1 A:HIS592 2.0 9.7 1.0
NE2 A:HIS433 2.1 10.2 1.0
O A:HOH2334 2.3 62.7 1.0
O A:HOH2332 2.6 28.1 1.0
CD2 A:HIS431 2.9 9.6 1.0
CE1 A:HIS431 3.0 11.1 1.0
CE1 A:HIS592 3.0 11.2 1.0
CG A:HIS592 3.0 11.4 1.0
CD2 A:HIS433 3.1 12.6 1.0
CE1 A:HIS433 3.1 11.6 1.0
HD2 A:HIS431 3.1 9.2 1.0
HB2 A:HIS592 3.1 8.4 1.0
HB3 A:HIS592 3.1 8.4 1.0
HE1 A:HIS592 3.2 10.9 1.0
HE1 A:HIS431 3.2 10.1 1.0
HD2 A:HIS433 3.2 11.1 1.0
HE1 A:HIS433 3.3 10.8 1.0
CB A:HIS592 3.3 8.0 1.0
O A:HOH2467 3.5 56.6 1.0
ND1 A:HIS431 4.1 7.6 1.0
CG A:HIS431 4.1 7.3 1.0
NE2 A:HIS592 4.1 11.2 1.0
CD2 A:HIS592 4.1 13.7 1.0
ND1 A:HIS433 4.2 9.3 1.0
CG A:HIS433 4.2 8.6 1.0
O A:HOH2235 4.4 27.7 1.0
HE3 A:MET602 4.5 21.2 0.5
O A:HOH2301 4.6 34.9 1.0
H3 A:TCQ382 4.6 22.9 1.0
HG3 A:PRO594 4.7 11.4 1.0
HE3 A:MET602 4.8 25.3 0.5
CA A:HIS592 4.8 7.9 1.0
O2 A:TCQ382 4.9 20.9 1.0
SD A:MET602 4.9 24.8 0.5
HG11 A:VAL406 4.9 17.8 1.0
SD A:MET602 4.9 25.6 0.5
HD2 A:HIS592 5.0 12.6 1.0

Copper binding site 2 out of 2 in 1w4n

Go back to Copper Binding Sites List in 1w4n
Copper binding site 2 out of 2 in the Agao Covalent Complex with Tranylcypromine


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Agao Covalent Complex with Tranylcypromine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:25.0
occ:1.00
ND1 B:HIS592 2.0 10.5 1.0
NE2 B:HIS433 2.0 6.3 1.0
NE2 B:HIS431 2.1 6.6 1.0
O B:HOH2358 2.3 40.8 1.0
O B:HOH2327 2.7 25.6 1.0
CE1 B:HIS592 2.9 9.7 1.0
CG B:HIS592 3.0 7.4 1.0
CE1 B:HIS433 3.0 8.2 1.0
CD2 B:HIS431 3.0 4.3 1.0
CD2 B:HIS433 3.0 9.2 1.0
CE1 B:HIS431 3.1 8.4 1.0
HE1 B:HIS592 3.1 9.3 1.0
HB3 B:HIS592 3.1 7.0 1.0
HD2 B:HIS431 3.1 4.4 1.0
HB2 B:HIS592 3.2 7.0 1.0
HD2 B:HIS433 3.2 8.0 1.0
HE1 B:HIS433 3.2 7.3 1.0
HE1 B:HIS431 3.3 7.1 1.0
CB B:HIS592 3.3 6.6 1.0
O B:HOH2503 3.5 50.0 1.0
NE2 B:HIS592 4.1 6.9 1.0
CD2 B:HIS592 4.1 10.6 1.0
ND1 B:HIS433 4.1 6.5 1.0
CG B:HIS433 4.1 7.2 1.0
ND1 B:HIS431 4.1 4.4 1.0
CG B:HIS431 4.1 2.7 1.0
O B:HOH2256 4.5 22.4 1.0
HE3 B:MET602 4.5 13.4 0.5
HG11 B:VAL406 4.6 16.2 1.0
O B:HOH2326 4.7 32.2 1.0
H3 B:TCQ382 4.7 13.4 1.0
HG3 B:PRO594 4.8 8.1 1.0
CA B:HIS592 4.8 7.2 1.0
SD B:MET602 4.9 19.4 0.5
HE3 B:MET602 4.9 14.8 0.5
SD B:MET602 4.9 22.7 0.5
HD2 B:HIS592 4.9 9.0 1.0
O2 B:TCQ382 5.0 14.0 1.0

Reference:

D.B.Langley, D.M.Trambaiolo, A.P.Duff, D.M.Dooley, H.C.Freeman, J.M.Guss. Complexes of the Copper-Containing Amine Oxidase From Arthrobacter Globiformis with the Inhibitors Benzylhydrazine and Tranylcypromine. Acta Crystallogr.,Sect.F V. 64 577 2008.
ISSN: ESSN 1744-3091
PubMed: 18607080
DOI: 10.1107/S174430910801556X
Page generated: Wed Oct 28 14:17:48 2020
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy