Zinc in PDB 1u5s: uc(Nmr) Structure of the Complex Between Nck-2 SH3 Domain and Pinch-1 LIM4 Domain

The binding sites of Zinc atom in the uc(Nmr) Structure of the Complex Between Nck-2 SH3 Domain and Pinch-1 LIM4 Domain (pdb code 1u5s). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the uc(Nmr) Structure of the Complex Between Nck-2 SH3 Domain and Pinch-1 LIM4 Domain, PDB code: 1u5s:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the uc(Nmr) Structure of the Complex Between Nck-2 SH3 Domain and Pinch-1 LIM4 Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of uc(Nmr) Structure of the Complex Between Nck-2 SH3 Domain and Pinch-1 LIM4 Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn138 b:0.0 occ:1.00 ND1 B:HIS99 2.0 0.0 1.0 ND1 B:HIS102 2.0 0.0 1.0 SG B:CYS79 2.3 0.0 1.0 SG B:CYS82 2.3 0.0 1.0 HB3 B:CYS79 2.5 0.0 1.0 CB B:CYS79 2.7 0.0 1.0 HB2 B:HIS99 2.7 0.0 1.0 HB2 B:CYS79 2.9 0.0 1.0 HB1 B:ALA81 2.9 0.0 1.0 HB2 B:HIS102 3.0 0.0 1.0 CE1 B:HIS102 3.0 0.0 1.0 CE1 B:HIS99 3.0 0.0 1.0 CG B:HIS99 3.0 0.0 1.0 CG B:HIS102 3.1 0.0 1.0 H B:CYS82 3.1 0.0 1.0 HE1 B:HIS102 3.2 0.0 1.0 HE1 B:HIS99 3.2 0.0 1.0 H B:HIS99 3.3 0.0 1.0 CB B:HIS99 3.4 0.0 1.0 CB B:HIS102 3.4 0.0 1.0 HB3 B:HIS102 3.8 0.0 1.0 N B:CYS82 3.8 0.0 1.0 CB B:ALA81 3.9 0.0 1.0 CB B:CYS82 3.9 0.0 1.0 HB2 B:ALA81 4.0 0.0 1.0 H B:ALA81 4.1 0.0 1.0 HB3 B:CYS82 4.1 0.0 1.0 N B:HIS99 4.1 0.0 1.0 HB3 B:HIS99 4.1 0.0 1.0 CD2 B:HIS99 4.1 0.0 1.0 NE2 B:HIS99 4.2 0.0 1.0 NE2 B:HIS102 4.2 0.0 1.0 CD2 B:HIS102 4.2 0.0 1.0 CA B:CYS79 4.2 0.0 1.0 HB2 B:ARG84 4.2 0.0 1.0 CA B:HIS99 4.4 0.0 1.0 CA B:CYS82 4.5 0.0 1.0 H B:ARG84 4.6 0.0 1.0 O B:CYS79 4.6 0.0 1.0 HB3 B:ALA81 4.6 0.0 1.0 C B:CYS79 4.6 0.0 1.0 C B:ALA81 4.6 0.0 1.0 HB2 B:CYS82 4.6 0.0 1.0 CA B:ALA81 4.7 0.0 1.0 H B:HIS102 4.7 0.0 1.0 N B:ALA81 4.7 0.0 1.0 HA B:CYS79 4.7 0.0 1.0 HG12 B:ILE86 4.7 0.0 1.0 H B:CYS79 4.8 0.0 1.0 CA B:HIS102 4.9 0.0 1.0 HD3 B:ARG84 4.9 0.0 1.0 H B:ARG83 4.9 0.0 1.0 HA B:TRP98 5.0 0.0 1.0 HA B:HIS99 5.0 0.0 1.0

Zinc binding site 2 out of 2 in the uc(Nmr) Structure of the Complex Between Nck-2 SH3 Domain and Pinch-1 LIM4 Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of uc(Nmr) Structure of the Complex Between Nck-2 SH3 Domain and Pinch-1 LIM4 Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn139 b:0.0 occ:1.00 ND1 B:HIS129 2.0 0.0 1.0 SG B:CYS108 2.3 0.0 1.0 SG B:CYS105 2.3 0.0 1.0 SG B:CYS126 2.3 0.0 1.0 H B:CYS126 2.5 0.0 1.0 HB2 B:CYS126 2.6 0.0 1.0 HB3 B:CYS105 2.6 0.0 1.0 HB2 B:CYS105 2.6 0.0 1.0 CB B:CYS105 2.7 0.0 1.0 CB B:CYS126 2.9 0.0 1.0 HB2 B:HIS129 2.9 0.0 1.0 CE1 B:HIS129 3.0 0.0 1.0 CG B:HIS129 3.1 0.0 1.0 HE1 B:HIS129 3.2 0.0 1.0 H B:CYS108 3.3 0.0 1.0 N B:CYS126 3.3 0.0 1.0 HB3 B:LYS107 3.4 0.0 1.0 HB3 B:CYS108 3.4 0.0 1.0 CB B:HIS129 3.5 0.0 1.0 CB B:CYS108 3.5 0.0 1.0 CA B:CYS126 3.7 0.0 1.0 N B:CYS108 3.8 0.0 1.0 HB3 B:CYS126 3.8 0.0 1.0 HB3 B:HIS129 3.9 0.0 1.0 H B:LYS107 4.1 0.0 1.0 H B:LYS110 4.1 0.0 1.0 HA B:TYR125 4.1 0.0 1.0 NE2 B:HIS129 4.2 0.0 1.0 HB2 B:LYS110 4.2 0.0 1.0 HB3 B:LYS110 4.2 0.0 1.0 H B:HIS129 4.2 0.0 1.0 CA B:CYS105 4.2 0.0 1.0 CD2 B:HIS129 4.2 0.0 1.0 H B:GLU109 4.2 0.0 1.0 HA B:CYS126 4.3 0.0 1.0 CA B:CYS108 4.3 0.0 1.0 HB2 B:CYS108 4.3 0.0 1.0 C B:TYR125 4.4 0.0 1.0 CB B:LYS107 4.4 0.0 1.0 HA B:CYS105 4.6 0.0 1.0 HD1 B:TYR125 4.6 0.0 1.0 C B:LYS107 4.7 0.0 1.0 CB B:LYS110 4.7 0.0 1.0 H B:CYS105 4.7 0.0 1.0 N B:LYS107 4.8 0.0 1.0 N B:GLU109 4.8 0.0 1.0 C B:CYS105 4.8 0.0 1.0 CA B:HIS129 4.8 0.0 1.0 CA B:TYR125 4.8 0.0 1.0 N B:HIS129 4.8 0.0 1.0 C B:CYS126 4.9 0.0 1.0 C B:CYS108 4.9 0.0 1.0 CA B:LYS107 4.9 0.0 1.0 N B:LYS110 4.9 0.0 1.0 HB2 B:LYS107 5.0 0.0 1.0 N B:CYS105 5.0 0.0 1.0

J.Vaynberg, T.Fukuda, K.Chen, O.Vinogradova, A.Velyvis, Y.Tu, L.Ng, C.Wu, J.Qin. Structure of An Ultraweak Protein-Protein Complex and Its Crucial Role in Regulation of Cell Morphology and Motility. Mol.Cell V. 17 513 2005.
ISSN: ISSN 1097-2765
PubMed: 15721255
DOI: 10.1016/J.MOLCEL.2004.12.031