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Manganese in PDB 1ksi: Crystal Structure of A Eukaryotic (Pea Seedling) Copper-Containing Amine Oxidase at 2.2A Resolution

Enzymatic activity of Crystal Structure of A Eukaryotic (Pea Seedling) Copper-Containing Amine Oxidase at 2.2A Resolution

All present enzymatic activity of Crystal Structure of A Eukaryotic (Pea Seedling) Copper-Containing Amine Oxidase at 2.2A Resolution:
1.4.3.6;

Protein crystallography data

The structure of Crystal Structure of A Eukaryotic (Pea Seedling) Copper-Containing Amine Oxidase at 2.2A Resolution, PDB code: 1ksi was solved by M.C.J.Wilce, V.Kumar, 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) 7.00 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 85.370, 114.640, 199.940, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1ksi:

The structure of Crystal Structure of A Eukaryotic (Pea Seedling) Copper-Containing Amine Oxidase at 2.2A Resolution also contains other interesting chemical elements:

Copper (Cu) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of A Eukaryotic (Pea Seedling) Copper-Containing Amine Oxidase at 2.2A Resolution (pdb code 1ksi). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of A Eukaryotic (Pea Seedling) Copper-Containing Amine Oxidase at 2.2A Resolution, PDB code: 1ksi:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1ksi

Go back to Manganese Binding Sites List in 1ksi
Manganese binding site 1 out of 2 in the Crystal Structure of A Eukaryotic (Pea Seedling) Copper-Containing Amine Oxidase at 2.2A Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of A Eukaryotic (Pea Seedling) Copper-Containing Amine Oxidase at 2.2A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn653

b:29.5
occ:1.00
OD1 A:ASP453 2.2 17.0 1.0
OD1 A:ASP592 2.3 22.1 1.0
O A:ILE593 2.3 12.9 1.0
OD1 A:ASP451 2.4 22.7 1.0
O A:PHE452 2.6 15.5 1.0
O A:HOH660 2.7 16.0 1.0
N A:ILE593 3.3 21.8 1.0
CG A:ASP592 3.4 22.8 1.0
CG A:ASP453 3.4 17.2 1.0
C A:ILE593 3.5 15.2 1.0
C A:PHE452 3.6 14.2 1.0
CG A:ASP451 3.6 20.4 1.0
NZ A:LYS48 3.7 21.4 1.0
OD2 A:ASP592 4.0 23.2 1.0
CA A:ILE593 4.1 17.1 1.0
C A:ASP592 4.1 23.6 1.0
OD2 A:ASP451 4.1 21.8 1.0
N A:PHE452 4.2 16.2 1.0
CA A:ASP592 4.2 23.4 1.0
OD2 A:ASP453 4.2 16.4 1.0
CA A:ASP453 4.3 15.6 1.0
N A:ASP453 4.3 13.3 1.0
C A:ASP451 4.3 16.3 1.0
CB A:ASP453 4.4 15.2 1.0
CB A:ASP592 4.5 22.4 1.0
CA A:PHE452 4.5 16.6 1.0
O A:THR457 4.5 23.2 1.0
O A:ASP451 4.6 16.3 1.0
N A:VAL594 4.6 14.9 1.0
CA A:ASP451 4.6 16.6 1.0
CB A:ASP451 4.7 17.6 1.0
CG1 A:ILE593 4.8 17.6 1.0
CG2 A:VAL594 4.8 13.4 1.0
CA A:VAL594 4.9 14.7 1.0
CE A:LYS48 4.9 23.5 1.0
OD1 A:ASN459 5.0 18.6 1.0

Manganese binding site 2 out of 2 in 1ksi

Go back to Manganese Binding Sites List in 1ksi
Manganese binding site 2 out of 2 in the Crystal Structure of A Eukaryotic (Pea Seedling) Copper-Containing Amine Oxidase at 2.2A Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of A Eukaryotic (Pea Seedling) Copper-Containing Amine Oxidase at 2.2A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn653

b:25.1
occ:1.00
OD1 B:ASP451 2.2 14.9 1.0
OD1 B:ASP453 2.2 15.3 1.0
O B:ILE593 2.3 12.2 1.0
OD1 B:ASP592 2.4 19.0 1.0
O B:HOH660 2.5 8.2 1.0
O B:PHE452 2.6 17.8 1.0
C B:ILE593 3.3 15.9 1.0
CG B:ASP451 3.4 15.8 1.0
N B:ILE593 3.4 19.7 1.0
CG B:ASP453 3.4 17.1 1.0
CG B:ASP592 3.4 20.4 1.0
C B:PHE452 3.5 16.9 1.0
NZ B:LYS48 3.9 19.5 1.0
OD2 B:ASP451 3.9 15.6 1.0
CA B:ILE593 4.0 16.6 1.0
C B:ASP592 4.0 21.2 1.0
OD2 B:ASP592 4.1 22.0 1.0
CA B:ASP592 4.1 20.7 1.0
N B:PHE452 4.2 17.7 1.0
CA B:ASP453 4.2 15.7 1.0
N B:ASP453 4.2 15.0 1.0
C B:ASP451 4.3 17.6 1.0
OD2 B:ASP453 4.3 16.6 1.0
O B:THR457 4.4 22.8 1.0
CB B:ASP453 4.4 16.3 1.0
CB B:ASP592 4.4 19.5 1.0
N B:VAL594 4.5 15.1 1.0
CA B:PHE452 4.5 17.3 1.0
CA B:ASP451 4.6 16.3 1.0
CB B:ASP451 4.6 15.2 1.0
O B:ASP451 4.6 14.3 1.0
CG2 B:VAL594 4.7 16.0 1.0
OD1 B:ASN459 4.8 11.9 1.0
CG1 B:ILE593 4.8 19.6 1.0
CA B:VAL594 4.9 16.0 1.0
O B:ASP592 5.0 23.4 1.0

Reference:

V.Kumar, D.M.Dooley, H.C.Freeman, J.M.Guss, I.Harvey, M.A.Mcguirl, M.C.Wilce, V.M.Zubak. Crystal Structure of A Eukaryotic (Pea Seedling) Copper-Containing Amine Oxidase at 2.2 A Resolution. Structure V. 4 943 1996.
ISSN: ISSN 0969-2126
PubMed: 8805580
DOI: 10.1016/S0969-2126(96)00101-3
Page generated: Tue Dec 15 03:51:45 2020

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