Zinc in PDB 7shk: Structure of Xenopus Laevis CRL2LRR1 (State 1)

The binding sites of Zinc atom in the Structure of Xenopus Laevis CRL2LRR1 (State 1) (pdb code 7shk). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Structure of Xenopus Laevis CRL2LRR1 (State 1), PDB code: 7shk:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Structure of Xenopus Laevis CRL2LRR1 (State 1)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Xenopus Laevis CRL2LRR1 (State 1) within 5.0Å range: probe atom residue distance (Å) B Occ L:Zn501 b:117.1 occ:1.00 SG L:CYS356 2.3 90.4 1.0 SG L:CYS358 2.3 94.8 1.0 SG L:CYS400 2.3 90.3 1.0 SG L:CYS404 2.3 93.8 1.0 CB L:CYS358 3.0 94.8 1.0 CB L:CYS404 3.3 93.8 1.0 CB L:CYS356 3.4 90.4 1.0 CB L:CYS400 3.6 90.3 1.0 N L:CYS358 3.8 94.8 1.0 N L:CYS400 3.9 90.3 1.0 CA L:CYS358 4.0 94.8 1.0 CA L:CYS400 4.3 90.3 1.0 N L:SER401 4.6 92.7 1.0 CA L:CYS356 4.7 90.4 1.0 CA L:CYS404 4.8 93.8 1.0 N L:ASP357 4.8 91.9 1.0 C L:CYS356 4.8 90.4 1.0 C L:CYS358 4.9 94.8 1.0 C L:PHE399 5.0 87.2 1.0

Zinc binding site 2 out of 4 in the Structure of Xenopus Laevis CRL2LRR1 (State 1)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Xenopus Laevis CRL2LRR1 (State 1) within 5.0Å range: probe atom residue distance (Å) B Occ R:Zn200 b:288.1 occ:1.00 ND1 R:HIS82 2.1 275.0 1.0 SG R:CYS56 2.3 263.2 1.0 SG R:CYS53 2.3 265.4 1.0 SG R:CYS68 2.3 270.2 1.0 CG R:HIS82 2.8 275.0 1.0 CB R:HIS82 3.1 275.0 1.0 CE1 R:HIS82 3.1 275.0 1.0 CB R:CYS56 3.2 263.2 1.0 CB R:CYS68 3.2 270.2 1.0 CB R:CYS53 3.6 265.4 1.0 CD2 R:HIS82 4.0 275.0 1.0 N R:CYS56 4.0 263.2 1.0 NE2 R:HIS82 4.1 275.0 1.0 CA R:CYS56 4.2 263.2 1.0 CA R:CYS68 4.2 270.2 1.0 CA R:HIS82 4.3 275.0 1.0 N R:HIS82 4.4 275.0 1.0 N R:CYS53 4.5 265.4 1.0 CA R:CYS53 4.6 265.4 1.0

Zinc binding site 3 out of 4 in the Structure of Xenopus Laevis CRL2LRR1 (State 1)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure of Xenopus Laevis CRL2LRR1 (State 1) within 5.0Å range: probe atom residue distance (Å) B Occ R:Zn201 b:289.0 occ:1.00 ND1 R:HIS80 2.3 271.1 1.0 SG R:CYS45 2.3 256.0 1.0 SG R:CYS83 2.3 272.2 1.0 SG R:CYS42 2.9 257.2 1.0 CG R:HIS80 3.1 271.1 1.0 CB R:HIS80 3.1 271.1 1.0 CB R:CYS83 3.2 272.2 1.0 CB R:CYS45 3.3 256.0 1.0 CE1 R:HIS80 3.4 271.1 1.0 CB R:CYS42 3.6 257.2 1.0 N R:CYS45 4.0 256.0 1.0 N R:HIS80 4.1 271.1 1.0 CB R:CYS53 4.1 265.4 1.0 CA R:HIS80 4.2 271.1 1.0 CA R:CYS45 4.2 256.0 1.0 CD2 R:HIS80 4.3 271.1 1.0 NE2 R:HIS80 4.4 271.1 1.0 CA R:CYS83 4.6 272.2 1.0 CA R:CYS53 4.8 265.4 1.0 CB R:ILE44 4.9 257.5 1.0 N R:CYS83 4.9 272.2 1.0

Zinc binding site 4 out of 4 in the Structure of Xenopus Laevis CRL2LRR1 (State 1)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structure of Xenopus Laevis CRL2LRR1 (State 1) within 5.0Å range: probe atom residue distance (Å) B Occ R:Zn202 b:293.8 occ:1.00 ND1 R:HIS77 2.3 276.7 1.0 SG R:CYS94 2.3 288.3 1.0 SG R:CYS75 2.3 279.9 1.0 CE1 R:HIS77 2.5 276.7 1.0 CB R:CYS75 2.9 279.9 1.0 OD1 R:ASP97 2.9 286.9 1.0 OD2 R:ASP97 3.0 286.9 1.0 CG R:ASP97 3.1 286.9 1.0 CB R:CYS94 3.1 288.3 1.0 CG R:HIS77 3.6 276.7 1.0 NE2 R:HIS77 3.8 276.7 1.0 CB R:LEU96 4.1 284.8 1.0 N R:ASP97 4.3 286.9 1.0 CA R:CYS75 4.3 279.9 1.0 CB R:ASP97 4.3 286.9 1.0 CD2 R:HIS77 4.4 276.7 1.0 CB R:HIS77 4.5 276.7 1.0 O R:CYS75 4.5 279.9 1.0 CA R:CYS94 4.6 288.3 1.0 CE3 R:TRP101 4.7 274.3 1.0 C R:CYS75 4.8 279.9 1.0 CZ3 R:TRP101 4.8 274.3 1.0 N R:LEU96 4.9 284.8 1.0 CA R:LEU96 4.9 284.8 1.0 C R:CYS94 4.9 288.3 1.0 C R:LEU96 4.9 284.8 1.0 CA R:ASP97 5.0 286.9 1.0 O R:CYS94 5.0 288.3 1.0

H.Zhou, M.S.Zaher, J.C.Walter, A.Brown. Structure of CRL2LRR1, the E3 Ubiquitin Ligase That Promotes Dna Replication Termination in Vertebrates. Nucleic Acids Res. 2021.
ISSN: ESSN 1362-4962
PubMed: 34850944
DOI: 10.1093/NAR/GKAB1174