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Cadmium in PDB 1oo2: Crystal Structure of Transthyretin From Sparus Aurata

Protein crystallography data

The structure of Crystal Structure of Transthyretin From Sparus Aurata, PDB code: 1oo2 was solved by N.Pasquato, I.Ramazzina, C.Folli, R.Battistutta, R.Berni, G.Zanotti, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.56
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 96.452, 65.622, 70.834, 90.00, 97.40, 90.00
R / Rfree (%) 19.7 / 22.4

Cadmium Binding Sites:

The binding sites of Cadmium atom in the Crystal Structure of Transthyretin From Sparus Aurata (pdb code 1oo2). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total 2 binding sites of Cadmium where determined in the Crystal Structure of Transthyretin From Sparus Aurata, PDB code: 1oo2:
Jump to Cadmium binding site number: 1; 2;

Cadmium binding site 1 out of 2 in 1oo2

Go back to Cadmium Binding Sites List in 1oo2
Cadmium binding site 1 out of 2 in the Crystal Structure of Transthyretin From Sparus Aurata


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 Transthyretin From Sparus Aurata within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cd401

b:29.7
occ:1.00
O C:HOH425 2.4 24.4 1.0
OE1 C:GLU72 2.4 21.4 1.0
O C:HOH467 2.6 24.8 1.0
O C:HOH502 3.2 78.4 1.0
CD C:GLU72 3.5 42.8 1.0
OE2 C:GLU72 3.9 27.6 1.0
O C:HOH448 4.2 22.7 1.0
O C:HOH435 4.3 29.1 1.0
O C:HOH449 4.3 28.3 1.0
O C:HOH410 4.7 17.7 1.0
CG C:GLU72 4.8 32.3 1.0
CB C:GLU72 5.0 14.9 1.0

Cadmium binding site 2 out of 2 in 1oo2

Go back to Cadmium Binding Sites List in 1oo2
Cadmium binding site 2 out of 2 in the Crystal Structure of Transthyretin From Sparus Aurata


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 Transthyretin From Sparus Aurata within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cd402

b:32.7
occ:1.00
OE1 C:GLU61 2.1 29.3 1.0
OE2 C:GLU61 2.2 46.9 1.0
NE2 C:HIS104 2.3 37.5 1.0
CD C:GLU61 2.4 34.3 1.0
O C:HOH470 2.4 43.6 1.0
O C:HOH479 2.6 37.5 1.0
CE1 C:HIS104 3.2 37.2 1.0
CD2 C:HIS104 3.3 34.0 1.0
CG C:GLU61 3.8 29.8 1.0
NE C:ARG9 3.8 74.6 1.0
NH2 C:ARG9 4.2 30.8 1.0
ND1 C:HIS104 4.3 38.9 1.0
CG C:HIS104 4.4 36.4 1.0
CZ C:ARG9 4.5 67.9 1.0
O C:ARG9 4.5 74.7 1.0
CB C:PRO11 4.7 24.6 1.0
CD C:ARG9 4.7 75.6 1.0
CB C:GLU61 4.8 34.0 1.0

Reference:

C.Folli, N.Pasquato, I.Ramazzina, R.Battistutta, G.Zanotti, R.Berni. Distinctive Binding and Structural Properties of Piscine Transthyretin. Febs Lett. V. 555 279 2003.
ISSN: ISSN 0014-5793
PubMed: 14644428
DOI: 10.1016/S0014-5793(03)01248-1
Page generated: Fri Aug 28 12:18:12 2020
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