Zinc in PDB 2ldr: Solution Structure of Helix-Ring Domain of Cbl-B in the TYR363 Phosphorylated Form

The binding sites of Zinc atom in the Solution Structure of Helix-Ring Domain of Cbl-B in the TYR363 Phosphorylated Form (pdb code 2ldr). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Solution Structure of Helix-Ring Domain of Cbl-B in the TYR363 Phosphorylated Form, PDB code: 2ldr:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Solution Structure of Helix-Ring Domain of Cbl-B in the TYR363 Phosphorylated Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution Structure of Helix-Ring Domain of Cbl-B in the TYR363 Phosphorylated Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1373 b:43.2 occ:1.00 SG A:CYS393 2.3 41.4 1.0 SG A:CYS396 2.3 10.1 1.0 SG A:CYS376 2.4 33.1 1.0 HB2 A:CYS393 2.6 53.1 1.0 HB3 A:CYS393 2.7 40.1 1.0 H A:ASN379 2.7 22.4 1.0 CB A:CYS393 2.7 64.4 1.0 SG A:CYS373 2.7 12.0 1.0 HB2 A:ASN379 2.8 71.1 1.0 CB A:ASN379 3.5 31.4 1.0 N A:ASN379 3.5 10.2 1.0 HB3 A:CYS373 3.5 52.1 1.0 HD21 A:ASN379 3.6 54.1 1.0 H A:GLU378 3.6 63.5 1.0 O A:ASN379 3.6 74.3 1.0 CB A:CYS373 3.7 12.2 1.0 CG A:ASN379 3.7 54.1 1.0 ND2 A:ASN379 3.7 32.3 1.0 CA A:ASN379 3.9 63.0 1.0 HB2 A:CYS373 3.9 55.2 1.0 H A:CYS376 3.9 33.4 1.0 C A:ASN379 3.9 61.4 1.0 HB3 A:GLU378 4.0 74.2 1.0 CB A:CYS376 4.0 44.2 1.0 CB A:CYS396 4.1 64.2 1.0 HB3 A:CYS376 4.2 12.2 1.0 CA A:CYS393 4.2 13.0 1.0 O A:ASP380 4.3 21.5 1.0 HD22 A:ASN379 4.3 31.3 1.0 OD1 A:ASN379 4.4 63.3 1.0 HB3 A:ASN379 4.5 52.2 1.0 HB3 A:CYS396 4.5 44.4 1.0 HB3 A:SER395 4.5 1.2 1.0 N A:GLU378 4.5 3.4 1.0 H A:CYS396 4.6 13.1 1.0 HB2 A:CYS396 4.6 12.3 1.0 H A:ALA377 4.6 4.4 1.0 H A:CYS393 4.6 3.1 1.0 C A:GLU378 4.7 55.5 1.0 N A:CYS376 4.7 30.4 1.0 HB2 A:CYS376 4.7 52.4 1.0 HA A:CYS393 4.8 33.2 1.0 CA A:CYS376 4.8 64.4 1.0 HB A:ILE375 4.8 62.1 1.0 N A:ASP380 4.9 73.5 1.0 CB A:GLU378 4.9 62.1 1.0 N A:CYS393 4.9 40.2 1.0 HA A:ASN379 4.9 54.3 1.0 N A:ALA377 4.9 74.5 1.0 N A:CYS396 5.0 62.2 1.0 CA A:GLU378 5.0 61.1 1.0 C A:CYS393 5.0 43.0 1.0 O A:CYS393 5.0 63.4 1.0 H A:CYS373 5.0 0.3 1.0

Zinc binding site 2 out of 2 in the Solution Structure of Helix-Ring Domain of Cbl-B in the TYR363 Phosphorylated Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Solution Structure of Helix-Ring Domain of Cbl-B in the TYR363 Phosphorylated Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1388 b:32.0 occ:1.00 ND1 A:HIS390 2.1 4.2 1.0 SG A:CYS408 2.3 61.1 1.0 SG A:CYS411 2.4 32.1 1.0 HB2 A:PHE410 2.4 11.5 1.0 HB2 A:HIS390 2.5 43.5 1.0 HB3 A:CYS408 2.6 75.3 1.0 SG A:CYS388 2.7 72.5 1.0 CG A:HIS390 2.9 2.3 1.0 HG22 A:ILE385 3.0 15.3 1.0 CB A:CYS408 3.0 62.1 1.0 CE1 A:HIS390 3.1 72.0 1.0 CB A:HIS390 3.1 64.2 1.0 H A:CYS411 3.1 43.3 1.0 HB2 A:CYS408 3.3 5.3 1.0 HB3 A:PHE410 3.4 51.0 1.0 CB A:PHE410 3.4 55.1 1.0 HE1 A:HIS390 3.5 60.2 1.0 HB3 A:HIS390 3.6 21.1 1.0 HB3 A:CYS388 3.6 14.5 1.0 N A:CYS411 3.7 62.2 1.0 CB A:CYS388 3.7 54.5 1.0 H A:PHE410 3.7 1.2 1.0 CB A:CYS411 3.8 23.3 1.0 HB2 A:CYS388 3.8 41.1 1.0 HB3 A:CYS411 3.9 21.0 1.0 HB A:ILE385 3.9 44.1 1.0 CG2 A:ILE385 4.0 54.4 1.0 CD2 A:HIS390 4.0 12.1 1.0 NE2 A:HIS390 4.1 14.3 1.0 H A:HIS390 4.2 25.3 1.0 C A:PHE410 4.2 62.1 1.0 CA A:PHE410 4.2 71.4 1.0 CA A:CYS411 4.3 3.2 1.0 CA A:CYS408 4.4 43.0 1.0 HG13 A:ILE385 4.4 25.3 1.0 N A:PHE410 4.4 0.3 1.0 CG A:PHE410 4.4 25.2 1.0 CA A:HIS390 4.4 44.5 1.0 CB A:ILE385 4.5 71.1 1.0 HG21 A:ILE385 4.6 33.1 1.0 N A:HIS390 4.6 11.5 1.0 HG23 A:ILE385 4.6 54.1 1.0 HB2 A:CYS411 4.6 74.1 1.0 HE3 A:MET392 4.7 5.3 1.0 C A:CYS408 4.7 61.3 1.0 H A:GLY389 4.8 44.2 1.0 HA A:CYS408 4.8 61.2 1.0 O A:CYS408 4.9 65.3 1.0 HD2 A:PHE410 4.9 10.5 1.0 HD2 A:HIS390 5.0 73.0 1.0

Y.Kobashigawa, A.Tomitaka, H.Kumeta, N.N.Noda, M.Yamaguchi, F.Inagaki. Autoinhibition and Phosphorylation-Induced Activation Mechanisms of Human Cancer and Autoimmune Disease-Related E3 Protein Cbl-B Proc.Natl.Acad.Sci.Usa V. 108 20579 2011.
ISSN: ISSN 0027-8424
PubMed: 22158902
DOI: 10.1073/PNAS.1110712108