Copper in PDB 8qy9: J22.9-H, Fully Humanized Fab Fragment Based on Chimeric J22.9-XI Igg Against Bcma

The structure of J22.9-H, Fully Humanized Fab Fragment Based on Chimeric J22.9-XI Igg Against Bcma, PDB code: 8qy9 was solved by S.F.Marino, O.Daumke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.78 / 3.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	137.36, 55.18, 81.16, 90, 121.02, 90
R / Rfree (%)	26.1 / 31.1

The binding sites of Copper atom in the J22.9-H, Fully Humanized Fab Fragment Based on Chimeric J22.9-XI Igg Against Bcma (pdb code 8qy9). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the J22.9-H, Fully Humanized Fab Fragment Based on Chimeric J22.9-XI Igg Against Bcma, PDB code: 8qy9:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the J22.9-H, Fully Humanized Fab Fragment Based on Chimeric J22.9-XI Igg Against Bcma


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of J22.9-H, Fully Humanized Fab Fragment Based on Chimeric J22.9-XI Igg Against Bcma within 5.0Å range: probe atom residue distance (Å) B Occ L:Cu301 b:93.6 occ:1.00 H1 L:GLU1 1.4 122.8 1.0 N L:GLU1 2.0 102.4 1.0 H2 L:GLU1 2.2 122.8 1.0 HA L:GLU1 2.4 112.1 1.0 CA L:GLU1 2.6 93.4 1.0 H3 L:GLU1 2.8 122.8 1.0 C L:GLU1 3.2 86.8 1.0 O L:GLU1 3.2 86.0 1.0 CB L:GLU1 4.0 85.0 1.0 N L:ILE2 4.2 84.3 1.0 HG3 L:GLU1 4.2 102.2 1.0 HG2 L:GLU1 4.3 102.2 1.0 CG L:GLU1 4.5 85.2 1.0 HB2 L:GLU1 4.5 102.0 1.0 HB3 L:GLU1 4.6 102.0 1.0 H L:ILE2 4.6 101.1 1.0 HG13 L:ILE2 4.8 92.1 1.0

Copper binding site 2 out of 2 in the J22.9-H, Fully Humanized Fab Fragment Based on Chimeric J22.9-XI Igg Against Bcma


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of J22.9-H, Fully Humanized Fab Fragment Based on Chimeric J22.9-XI Igg Against Bcma within 5.0Å range: probe atom residue distance (Å) B Occ H:Cu301 b:111.1 occ:1.00 HD21 L:ASN137 1.6 119.4 1.0 NE2 H:HIS171 2.0 84.6 1.0 OD1 L:ASN137 2.1 90.2 1.0 ND2 L:ASN137 2.2 99.5 1.0 CG L:ASN137 2.4 89.7 1.0 CD2 H:HIS171 2.5 74.8 1.0 HD2 H:HIS171 2.5 89.8 1.0 HD22 L:ASN137 3.0 119.4 1.0 CE1 H:HIS171 3.2 77.8 1.0 HA2 H:GLY169 3.4 86.7 1.0 HE1 H:HIS171 3.6 93.4 1.0 HB2 L:ASN138 3.7 88.6 1.0 CG H:HIS171 3.7 73.3 1.0 CB L:ASN137 3.9 81.1 1.0 O H:GLY169 3.9 74.8 1.0 HG1 H:THR190 3.9 89.7 1.0 ND1 H:HIS171 4.0 73.0 1.0 HG23 H:THR190 4.2 90.2 1.0 H L:ASN138 4.2 79.2 1.0 HB2 L:ASN137 4.2 97.3 1.0 CA H:GLY169 4.3 72.2 1.0 HB3 L:ASN137 4.3 97.3 1.0 C H:GLY169 4.4 72.4 1.0 OG L:SER174 4.4 78.5 1.0 OG1 H:THR190 4.4 74.7 1.0 N L:ASN138 4.5 66.0 1.0 HG21 H:THR190 4.5 90.2 1.0 HA3 H:GLY169 4.5 86.7 1.0 CB L:ASN138 4.6 73.8 1.0 HA L:ASN137 4.7 87.3 1.0 HG L:SER174 4.7 94.1 1.0 CG2 H:THR190 4.8 75.2 1.0 CA L:ASN137 4.8 72.7 1.0 HD1 H:HIS171 4.8 87.6 1.0 C L:ASN137 4.9 65.6 1.0 HB3 L:ASN138 4.9 88.6 1.0 HB2 H:HIS171 5.0 98.8 1.0 CA L:ASN138 5.0 68.2 1.0 HA L:ASN138 5.0 81.9 1.0

S.F.Marino, O.Daumke. Structure-Based Humanization of A Therapeutic Antibody For Multiple Myeloma To Be Published.