Zinc in PDB 1u6g: Crystal Structure of the CAND1-CUL1-ROC1 Complex

The structure of Crystal Structure of the CAND1-CUL1-ROC1 Complex, PDB code: 1u6g was solved by S.J.Goldenberg, S.D.Shumway, T.C.Cascio, K.C.Garbutt, J.Liu, Y.Xiong, N.Zheng, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 3.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	108.466, 151.327, 215.892, 90.00, 90.00, 90.00
R / Rfree (%)	24.3 / 31.7

The binding sites of Zinc atom in the Crystal Structure of the CAND1-CUL1-ROC1 Complex (pdb code 1u6g). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of the CAND1-CUL1-ROC1 Complex, PDB code: 1u6g:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Crystal Structure of the CAND1-CUL1-ROC1 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the CAND1-CUL1-ROC1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1229 b:42.5 occ:1.00 ND1 B:HIS80 1.9 38.8 1.0 SG B:CYS45 1.9 35.4 1.0 SG B:CYS42 2.2 23.4 1.0 SG B:CYS83 2.2 29.1 1.0 CG B:HIS80 2.8 35.6 1.0 CB B:CYS83 2.9 25.2 1.0 CE1 B:HIS80 2.9 38.3 1.0 CB B:CYS42 2.9 28.5 1.0 CB B:HIS80 3.2 31.8 1.0 CB B:CYS45 3.6 37.3 1.0 N B:HIS80 3.8 24.1 1.0 CD2 B:HIS80 4.0 37.7 1.0 NE2 B:HIS80 4.0 38.4 1.0 CA B:HIS80 4.1 24.8 1.0 O B:CYS45 4.1 42.5 1.0 N B:CYS45 4.1 39.9 1.0 CB B:CYS53 4.2 33.1 1.0 CA B:CYS53 4.3 19.9 1.0 CA B:CYS83 4.3 39.8 1.0 CA B:CYS42 4.4 49.2 1.0 CA B:CYS45 4.5 40.7 1.0 N B:CYS83 4.6 39.2 1.0 C B:CYS42 4.7 48.3 1.0 C B:CYS45 4.7 42.6 1.0 O B:CYS42 4.8 48.1 1.0 CB B:ILE44 4.9 6.5 1.0 O B:HIS80 4.9 25.0 1.0 C B:PHE79 4.9 40.1 1.0 N B:ILE44 5.0 18.9 1.0

Zinc binding site 2 out of 3 in the Crystal Structure of the CAND1-CUL1-ROC1 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the CAND1-CUL1-ROC1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1230 b:56.4 occ:1.00 ND1 B:HIS77 2.0 26.8 1.0 SG B:CYS94 2.1 24.3 1.0 OD2 B:ASP97 2.2 20.0 1.0 SG B:CYS75 2.2 28.9 1.0 CG B:HIS77 2.7 26.7 1.0 CB B:HIS77 2.7 25.6 1.0 CE1 B:HIS77 3.2 25.2 1.0 CG B:ASP97 3.3 20.0 1.0 CB B:CYS75 3.4 26.0 1.0 CB B:CYS94 3.6 28.5 1.0 CB B:ASP97 3.8 46.5 1.0 N B:HIS77 3.9 41.4 1.0 CA B:HIS77 3.9 40.4 1.0 CD2 B:HIS77 3.9 26.0 1.0 NE2 B:HIS77 4.2 24.4 1.0 OD1 B:ASP97 4.4 20.0 1.0 C B:CYS75 4.4 27.0 1.0 CA B:CYS75 4.5 25.8 1.0 O B:CYS75 4.5 27.3 1.0 N B:ASP97 4.7 47.0 1.0 CZ3 B:TRP101 4.8 11.7 1.0 N B:ASN76 4.8 33.2 1.0 CA B:ASP97 4.8 49.0 1.0 CA B:CYS94 4.8 26.7 1.0 C B:HIS77 4.8 37.2 1.0 C B:ASN76 4.9 32.2 1.0 O B:HIS77 4.9 34.3 1.0 CE3 B:TRP101 4.9 14.0 1.0 CB B:LEU96 4.9 36.5 1.0 C B:LEU96 5.0 41.2 1.0

Zinc binding site 3 out of 3 in the Crystal Structure of the CAND1-CUL1-ROC1 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the CAND1-CUL1-ROC1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1231 b:36.6 occ:1.00 ND1 B:HIS82 2.0 41.2 1.0 SG B:CYS56 2.1 29.1 1.0 SG B:CYS68 2.1 26.6 1.0 SG B:CYS53 2.1 25.4 1.0 CE1 B:HIS82 2.9 39.2 1.0 CG B:HIS82 3.1 40.2 1.0 CB B:CYS56 3.2 37.4 1.0 CB B:CYS68 3.4 21.6 1.0 CB B:CYS53 3.5 33.1 1.0 CB B:HIS82 3.6 39.4 1.0 N B:CYS53 3.9 20.5 1.0 N B:CYS56 4.1 82.3 1.0 CA B:CYS68 4.1 32.5 1.0 NE2 B:HIS82 4.1 39.8 1.0 CD2 B:HIS82 4.2 40.0 1.0 CA B:CYS56 4.3 80.1 1.0 CA B:CYS53 4.3 19.9 1.0 O B:CYS53 4.6 23.3 1.0 C B:CYS53 4.8 22.0 1.0 CB B:LEU52 4.9 20.4 1.0 NH2 B:ARG86 4.9 28.8 1.0 N B:CYS68 4.9 35.1 1.0 C B:LEU52 5.0 11.2 1.0 CA B:HIS82 5.0 20.9 1.0

S.J.Goldenberg, T.C.Cascio, S.D.Shumway, K.C.Garbutt, J.Liu, Y.Xiong, N.Zheng. Structure of the CAND1-CUL1-ROC1 Complex Reveals Regulatory Mechanisms For the Assembly of the Multisubunit Cullin-Dependent Ubiquitin Ligases Cell(Cambridge,Mass.) V. 119 517 2004.
ISSN: ISSN 0092-8674
PubMed: 15537541
DOI: 10.1016/J.CELL.2004.10.019