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Cadmium in PDB 2xdv: Crystal Structure of the Catalytic Domain of FLJ14393

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of FLJ14393, PDB code: 2xdv was solved by T.Krojer, J.R.C.Muniz, S.S.Ng, E.Pilka, K.Guo, A.C.W.Pike, P.Filippakopoulos, S.Knapp, K.L.Kavanagh, O.Gileadi, G.Bunkoczi, W.W.Yue, F.Niesen, F.Sobott, O.Fedorov, P.Savitsky, G.Kochan, M.Daniel, F.Vondelft, C.H.Arrowsmith, A.M.Edwards, J.Weigelt, C.Bountra, U.Oppermann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.28 / 2.57
Space group P 43 3 2
Cell size a, b, c (Å), α, β, γ (°) 185.180, 185.180, 185.180, 90.00, 90.00, 90.00
R / Rfree (%) 19.7 / 22.9

Other elements in 2xdv:

The structure of Crystal Structure of the Catalytic Domain of FLJ14393 also contains other interesting chemical elements:

Nickel (Ni) 6 atoms
Manganese (Mn) 1 atom

Cadmium Binding Sites:

The binding sites of Cadmium atom in the Crystal Structure of the Catalytic Domain of FLJ14393 (pdb code 2xdv). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total 3 binding sites of Cadmium where determined in the Crystal Structure of the Catalytic Domain of FLJ14393, PDB code: 2xdv:
Jump to Cadmium binding site number: 1; 2; 3;

Cadmium binding site 1 out of 3 in 2xdv

Go back to Cadmium Binding Sites List in 2xdv
Cadmium binding site 1 out of 3 in the Crystal Structure of the Catalytic Domain of FLJ14393


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 Catalytic Domain of FLJ14393 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cd1476

b:68.4
occ:1.00
O A:HOH2133 2.3 52.2 1.0
NE2 A:HIS371 2.5 59.8 1.0
OD1 A:ASP370 2.5 82.1 1.0
OD2 A:ASP370 2.7 82.4 1.0
O A:HOH2057 2.7 66.2 1.0
SG A:CYS156 2.9 63.6 1.0
CG A:ASP370 2.9 79.8 1.0
CD2 A:HIS371 3.2 59.4 1.0
CB A:CYS156 3.5 56.9 1.0
CE1 A:HIS371 3.7 59.3 1.0
CA A:CYS156 4.2 53.1 1.0
O A:HOH2030 4.3 61.5 1.0
NH2 A:ARG338 4.5 49.2 1.0
CB A:ASP370 4.5 64.3 1.0
CG A:HIS371 4.5 57.1 1.0
NH1 A:ARG338 4.7 49.2 1.0
ND1 A:HIS371 4.7 59.1 1.0

Cadmium binding site 2 out of 3 in 2xdv

Go back to Cadmium Binding Sites List in 2xdv
Cadmium binding site 2 out of 3 in the Crystal Structure of the Catalytic Domain of FLJ14393


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 2 of Crystal Structure of the Catalytic Domain of FLJ14393 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cd1477

b:0.3
occ:1.00
O A:HOH2021 3.0 68.3 1.0
CB A:LYS87 4.3 0.2 1.0

Cadmium binding site 3 out of 3 in 2xdv

Go back to Cadmium Binding Sites List in 2xdv
Cadmium binding site 3 out of 3 in the Crystal Structure of the Catalytic Domain of FLJ14393


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 3 of Crystal Structure of the Catalytic Domain of FLJ14393 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cd1478

b:0.9
occ:1.00
SG A:CYS460 2.8 68.7 1.0
O A:HOH2147 4.1 54.5 1.0
CB A:CYS460 4.1 62.5 1.0
CD A:LYS398 4.8 89.8 1.0
NZ A:LYS398 4.9 0.1 1.0
CE A:LYS398 4.9 99.7 1.0

Reference:

R.Chowdhury, R.Sekirnik, N.C.Brissett, T.Krojer, C.H.Ho, S.S.Ng, I.J.Clifton, W.Ge, N.J.Kershaw, G.C.Fox, J.R.C.Muniz, M.Vollmar, C.Phillips, E.S.Pilka, K.L.Kavanagh, F.Von Delft, U.Oppermann, M.A.Mcdonough, A.J.Doherty, C.J.Schofield. Ribosomal Oxygenases Are Structurally Conserved From Prokaryotes to Humans. Nature V. 510 422 2014.
ISSN: ESSN 1476-4687
PubMed: 24814345
DOI: 10.1038/NATURE13263
Page generated: Thu Jul 10 12:13:34 2025

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