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Cadmium in PDB 3liz: Crystal Structure of Bla G 2 Complexed with Fab 4C3

Protein crystallography data

The structure of Crystal Structure of Bla G 2 Complexed with Fab 4C3, PDB code: 3liz was solved by M.Li, A.Gustchina, J.Glesner, S.Wunschmann, A.Pomes, A.Wlodawer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.49 / 1.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 155.213, 105.285, 109.154, 90.00, 132.58, 90.00
R / Rfree (%) 17.7 / 20.2

Other elements in 3liz:

The structure of Crystal Structure of Bla G 2 Complexed with Fab 4C3 also contains other interesting chemical elements:

Zinc (Zn) 7 atoms

Cadmium Binding Sites:

The binding sites of Cadmium atom in the Crystal Structure of Bla G 2 Complexed with Fab 4C3 (pdb code 3liz). 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 Bla G 2 Complexed with Fab 4C3, PDB code: 3liz:
Jump to Cadmium binding site number: 1; 2; 3;

Cadmium binding site 1 out of 3 in 3liz

Go back to Cadmium Binding Sites List in 3liz
Cadmium binding site 1 out of 3 in the Crystal Structure of Bla G 2 Complexed with Fab 4C3


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 Bla G 2 Complexed with Fab 4C3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cd330

b:24.9
occ:0.90
OE2 A:GLU327 2.3 32.8 1.0
ND1 A:HIS308 2.3 25.6 1.0
O A:HOH447 2.4 13.7 1.0
O A:HOH347 2.4 21.6 1.0
OE1 A:GLU327 2.5 31.6 1.0
O A:HOH361 2.5 28.0 1.0
CD A:GLU327 2.7 33.0 1.0
CE1 A:HIS308 3.2 27.8 1.0
CG A:HIS308 3.3 22.5 1.0
CB A:HIS308 3.6 22.3 1.0
NE A:ARG324 4.2 30.9 1.0
CA A:HIS308 4.2 21.3 1.0
CG A:GLU327 4.3 33.6 1.0
O A:HOH600 4.3 44.3 1.0
O A:HOH349 4.4 44.4 1.0
NE2 A:HIS308 4.4 23.8 1.0
CD2 A:HIS308 4.4 24.1 1.0
O A:HIS308 4.5 20.4 1.0
NH2 A:ARG324 4.5 31.8 1.0
O A:HOH454 4.5 43.1 1.0
C8 A:NAG501 4.5 26.8 1.0
O3 A:NAG501 4.6 29.4 1.0
O A:SER325 4.6 26.8 1.0
N2 A:NAG501 4.6 26.2 1.0
CG A:ARG324 4.7 27.0 1.0
CZ A:ARG324 4.8 33.9 1.0
C A:HIS308 4.9 21.1 1.0
C3 A:NAG501 4.9 29.3 1.0
C7 A:NAG501 4.9 27.9 1.0
OH A:TYR273 4.9 28.8 1.0

Cadmium binding site 2 out of 3 in 3liz

Go back to Cadmium Binding Sites List in 3liz
Cadmium binding site 2 out of 3 in the Crystal Structure of Bla G 2 Complexed with Fab 4C3


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 Bla G 2 Complexed with Fab 4C3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cd331

b:21.2
occ:0.80
O A:HOH448 2.0 19.2 1.0
O A:HOH449 2.0 13.9 1.0
ND1 A:HIS3 2.3 24.4 1.0
O A:HOH345 2.6 12.4 1.0
CE1 A:HIS3 3.2 24.6 1.0
CG A:HIS3 3.4 24.9 1.0
O A:HOH787 3.7 0.5 1.0
CB A:HIS3 3.8 24.8 1.0
N A:HIS3 4.0 24.4 1.0
NE2 A:HIS3 4.4 25.8 1.0
CD2 A:HIS3 4.5 22.5 1.0
O A:HOH468 4.5 44.0 1.0
O A:LEU1 4.5 22.6 1.0
CA A:HIS3 4.5 24.2 1.0
C A:VAL2 4.9 22.6 1.0
CA A:VAL2 4.9 22.3 1.0

Cadmium binding site 3 out of 3 in 3liz

Go back to Cadmium Binding Sites List in 3liz
Cadmium binding site 3 out of 3 in the Crystal Structure of Bla G 2 Complexed with Fab 4C3


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 Bla G 2 Complexed with Fab 4C3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cd332

b:28.0
occ:1.00
OE2 A:GLU142 2.1 32.5 1.0
OE2 A:GLU138 2.3 27.6 1.0
CD A:GLU142 3.2 31.9 1.0
CD A:GLU138 3.2 30.3 1.0
CG A:GLU138 3.4 28.1 1.0
CG A:GLU142 3.7 28.8 1.0
O A:HOH522 4.1 38.0 1.0
OE1 A:GLU142 4.2 32.9 1.0
OE1 A:GLU138 4.3 25.2 1.0
CE A:LYS134 4.5 30.2 1.0
NZ A:LYS134 4.5 33.9 1.0
CB A:GLU138 4.9 24.3 1.0
CD A:LYS134 4.9 29.3 1.0

Reference:

J.Glesner, S.Wunschmann, M.Li, A.Gustchina, A.Wlodawer, M.Himly, M.D.Chapman, A.Pomes. Mechanisms of Allergen-Antibody Interaction of Cockroach Allergen Bla G 2 with Monoclonal Antibodies That Inhibit Ige Antibody Binding. Plos One V. 6 22223 2011.
ISSN: ESSN 1932-6203
PubMed: 21789239
DOI: 10.1371/JOURNAL.PONE.0022223
Page generated: Sat Dec 12 08:22:28 2020

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