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Cadmium in PDB 3cjk: Crystal Structure of the Adduct HAH1-Cd(II)-MNK1.

Enzymatic activity of Crystal Structure of the Adduct HAH1-Cd(II)-MNK1.

All present enzymatic activity of Crystal Structure of the Adduct HAH1-Cd(II)-MNK1.:
3.6.3.4;

Protein crystallography data

The structure of Crystal Structure of the Adduct HAH1-Cd(II)-MNK1., PDB code: 3cjk was solved by L.Banci, I.Bertini, V.Calderone, I.Felli, N.Della-Malva, A.Pavelkova, A.Rosato, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.30 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.707, 55.274, 63.241, 90.00, 90.00, 90.00
R / Rfree (%) 22.6 / 28.3

Cadmium Binding Sites:

The binding sites of Cadmium atom in the Crystal Structure of the Adduct HAH1-Cd(II)-MNK1. (pdb code 3cjk). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total only one binding site of Cadmium was determined in the Crystal Structure of the Adduct HAH1-Cd(II)-MNK1., PDB code: 3cjk:

Cadmium binding site 1 out of 1 in 3cjk

Go back to Cadmium Binding Sites List in 3cjk
Cadmium binding site 1 out of 1 in the Crystal Structure of the Adduct HAH1-Cd(II)-MNK1.


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 1 of Crystal Structure of the Adduct HAH1-Cd(II)-MNK1. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cd1

b:24.4
occ:1.00
OG1 B:THR14 2.5 19.3 1.0
SG B:CYS18 2.5 26.8 1.0
SG B:CYS15 2.5 26.4 1.0
SG A:CYS12 2.5 18.6 1.0
N B:CYS15 3.5 30.4 1.0
CB A:CYS12 3.5 20.8 1.0
CB B:CYS18 3.5 23.3 1.0
N B:CYS18 3.6 24.2 1.0
CB B:CYS15 3.6 27.5 1.0
CB B:THR14 3.8 31.1 1.0
CA B:CYS15 3.9 28.6 1.0
N B:THR14 4.0 32.6 1.0
C B:THR14 4.1 31.4 1.0
O B:CYS15 4.1 27.0 1.0
CA B:CYS18 4.1 22.1 1.0
CA A:GLY14 4.1 20.9 1.0
N A:GLY14 4.2 21.6 1.0
CA B:THR14 4.2 30.8 1.0
C B:CYS15 4.2 27.9 1.0
CB B:SER17 4.5 25.3 1.0
C B:SER17 4.5 23.0 1.0
CG2 B:THR14 4.6 26.0 1.0
N A:CYS15 4.6 19.0 1.0
OG B:SER17 4.7 31.8 1.0
N B:SER17 4.7 24.6 1.0
CA B:SER17 4.8 24.9 1.0
C A:GLY14 4.8 20.4 1.0
O B:HOH118 4.9 24.9 1.0
CA A:CYS12 4.9 20.6 1.0
O B:THR14 4.9 33.3 1.0

Reference:

L.Banci, I.Bertini, V.Calderone, N.Della-Malva, I.C.Felli, S.Neri, A.Pavelkova, A.Rosato. Copper(I)-Mediated Protein-Protein Interactions Result From Suboptimal Interaction Surfaces. Biochem.J. V. 422 37 2009.
ISSN: ISSN 0264-6021
PubMed: 19453293
DOI: 10.1042/BJ20090422
Page generated: Fri Jul 19 15:46:43 2024

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