Zinc in PDB 8xma: Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation

The binding sites of Zinc atom in the Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation (pdb code 8xma). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation, PDB code: 8xma:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Zinc binding site 1 out of 8 in the Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:118.2 occ:1.00 OE2 B:GLU420 2.0 95.7 1.0 ND1 B:HIS387 2.0 82.4 1.0 NE2 B:HIS370 2.0 85.4 1.0 SG B:CYS433 2.3 105.9 1.0 CG B:HIS387 2.8 82.4 1.0 CE1 B:HIS370 2.8 85.4 1.0 CB B:HIS387 2.9 82.4 1.0 CD2 B:HIS370 3.0 85.4 1.0 CD B:GLU420 3.1 95.7 1.0 CE1 B:HIS387 3.2 82.4 1.0 CB B:CYS433 3.4 105.9 1.0 OE1 B:GLU420 3.7 95.7 1.0 ND1 B:HIS370 3.9 85.4 1.0 CG B:HIS370 4.0 85.4 1.0 CD2 B:HIS387 4.0 82.4 1.0 NE2 B:HIS387 4.2 82.4 1.0 NE2 B:GLN418 4.2 83.6 1.0 CA B:CYS433 4.2 105.9 1.0 CG B:GLU420 4.4 95.7 1.0 CA B:HIS387 4.4 82.4 1.0 CB B:GLU371 4.7 80.7 1.0 O B:HIS370 4.9 85.4 1.0

Zinc binding site 2 out of 8 in the Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn602 b:111.1 occ:1.00 ND1 B:HIS413 2.0 85.7 1.0 ND1 B:HIS408 2.0 92.9 1.0 SG A:CYS437 2.3 103.7 1.0 CB A:CYS437 2.8 103.7 1.0 CE1 B:HIS413 3.0 85.7 1.0 CG B:HIS408 3.0 92.9 1.0 CG B:HIS413 3.0 85.7 1.0 CE1 B:HIS408 3.0 92.9 1.0 CB B:HIS408 3.3 92.9 1.0 CB B:HIS413 3.4 85.7 1.0 CA B:HIS413 3.7 85.7 1.0 CA A:CYS437 3.8 103.7 1.0 CA B:HIS408 3.8 92.9 1.0 O B:ILE412 3.9 81.0 1.0 NE2 B:HIS413 4.1 85.7 1.0 CD2 B:HIS408 4.1 92.9 1.0 NE2 B:HIS408 4.1 92.9 1.0 CD2 B:HIS413 4.1 85.7 1.0 N B:HIS413 4.6 85.7 1.0 C B:ILE412 4.6 81.0 1.0 O B:HIS413 4.7 85.7 1.0 C A:CYS437 4.7 103.7 1.0 C B:HIS413 4.7 85.7 1.0 N A:CYS437 4.8 103.7 1.0 N B:HIS408 4.8 92.9 1.0 O B:HIS408 4.8 92.9 1.0 N A:ARG438 4.8 109.4 1.0 C B:HIS408 4.9 92.9 1.0

Zinc binding site 3 out of 8 in the Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn603 b:112.9 occ:1.00 OE2 B:GLU371 2.0 80.7 1.0 NE2 B:HIS373 2.0 67.6 1.0 SG B:CYS446 2.3 90.4 1.0 SG B:CYS447 2.3 86.3 1.0 CE1 B:HIS373 2.6 67.6 1.0 O B:CYS446 2.8 90.4 1.0 CD B:GLU371 3.1 80.7 1.0 C B:CYS446 3.1 90.4 1.0 CB B:CYS446 3.2 90.4 1.0 CD2 B:HIS373 3.3 67.6 1.0 CB B:CYS447 3.5 86.3 1.0 CA B:CYS446 3.7 90.4 1.0 N B:CYS447 3.7 86.3 1.0 OE1 B:GLU371 3.8 80.7 1.0 ND1 B:HIS373 3.8 67.6 1.0 CA B:CYS447 4.1 86.3 1.0 CG B:GLU371 4.2 80.7 1.0 CG B:HIS373 4.2 67.6 1.0 N B:CYS446 4.5 90.4 1.0 C B:CYS447 4.6 86.3 1.0 CD1 A:PHE72 5.0 61.5 1.0

Zinc binding site 4 out of 8 in the Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn604 b:110.6 occ:1.00 OD1 B:ASP47 2.0 83.6 1.0 OD1 B:ASP255 2.0 80.0 1.0 OD2 B:ASP47 2.0 83.6 1.0 NE2 B:HIS251 2.1 75.3 1.0 CG B:ASP47 2.1 83.6 1.0 OD2 B:ASP255 2.2 80.0 1.0 CG B:ASP255 2.4 80.0 1.0 CD2 B:HIS251 2.5 75.3 1.0 CE1 B:HIS251 3.3 75.3 1.0 CB B:ASP47 3.4 83.6 1.0 CG B:HIS251 3.8 75.3 1.0 CB B:ASP255 3.9 80.0 1.0 ND1 B:HIS251 4.1 75.3 1.0 O B:HIS251 4.1 75.3 1.0 CA B:ASP47 4.2 83.6 1.0 N B:ASP47 4.6 83.6 1.0 CA B:ASP255 4.7 80.0 1.0 OG B:SER46 4.8 82.9 1.0 C B:HIS251 4.9 75.3 1.0 N B:ASP255 4.9 80.0 1.0

Zinc binding site 5 out of 8 in the Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:108.8 occ:1.00 OE2 A:GLU420 2.0 97.9 1.0 ND1 A:HIS387 2.0 82.2 1.0 NE2 A:HIS370 2.1 85.9 1.0 SG A:CYS433 2.3 104.0 1.0 CB A:HIS387 2.5 82.2 1.0 CG A:HIS387 2.6 82.2 1.0 CD A:GLU420 2.7 97.9 1.0 CD2 A:HIS370 2.9 85.9 1.0 CE1 A:HIS370 3.0 85.9 1.0 OE1 A:GLU420 3.1 97.9 1.0 CE1 A:HIS387 3.3 82.2 1.0 CB A:CYS433 3.5 104.0 1.0 CD2 A:HIS387 3.8 82.2 1.0 CG A:GLU420 3.9 97.9 1.0 ND1 A:HIS370 4.0 85.9 1.0 CG A:HIS370 4.0 85.9 1.0 CA A:HIS387 4.0 82.2 1.0 NE2 A:HIS387 4.1 82.2 1.0 CA A:CYS433 4.3 104.0 1.0 NE2 A:GLN418 4.4 82.9 1.0 C A:HIS387 4.6 82.2 1.0 O A:HIS370 4.8 85.9 1.0 O A:PRO432 4.9 108.2 1.0 N A:HIS387 4.9 82.2 1.0

Zinc binding site 6 out of 8 in the Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn602 b:106.6 occ:1.00 ND1 A:HIS413 2.0 88.7 1.0 ND1 A:HIS408 2.0 93.7 1.0 SG B:CYS437 2.3 107.5 1.0 CG A:HIS408 2.9 93.7 1.0 CG A:HIS413 3.0 88.7 1.0 CE1 A:HIS413 3.1 88.7 1.0 CE1 A:HIS408 3.1 93.7 1.0 CB A:HIS408 3.2 93.7 1.0 CB B:CYS437 3.2 107.5 1.0 CB A:HIS413 3.2 88.7 1.0 CA A:HIS413 3.5 88.7 1.0 CA A:HIS408 3.7 93.7 1.0 O A:ILE412 3.8 83.4 1.0 CA B:CYS437 4.0 107.5 1.0 CD2 A:HIS408 4.1 93.7 1.0 CD2 A:HIS413 4.1 88.7 1.0 NE2 A:HIS408 4.1 93.7 1.0 NE2 A:HIS413 4.1 88.7 1.0 N A:HIS413 4.4 88.7 1.0 C A:ILE412 4.5 83.4 1.0 O A:HIS413 4.5 88.7 1.0 C A:HIS413 4.5 88.7 1.0 N A:HIS408 4.6 93.7 1.0 C A:HIS408 4.7 93.7 1.0 O A:HIS408 4.8 93.7 1.0 N B:ARG438 4.9 111.2 1.0 C B:CYS437 4.9 107.5 1.0 N B:CYS437 5.0 107.5 1.0

Zinc binding site 7 out of 8 in the Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn603 b:108.2 occ:1.00 OE2 A:GLU371 2.0 82.8 1.0 NE2 A:HIS373 2.0 66.7 1.0 SG A:CYS446 2.3 86.0 1.0 SG A:CYS447 2.4 81.8 1.0 CD A:GLU371 2.4 82.8 1.0 CG A:GLU371 2.5 82.8 1.0 CE1 A:HIS373 2.9 66.7 1.0 CD2 A:HIS373 3.1 66.7 1.0 O A:CYS446 3.2 86.0 1.0 OE1 A:GLU371 3.5 82.8 1.0 C A:CYS446 3.6 86.0 1.0 CB A:CYS446 3.6 86.0 1.0 CB A:CYS447 3.7 81.8 1.0 CB A:GLU371 3.8 82.8 1.0 ND1 A:HIS373 4.0 66.7 1.0 CG A:HIS373 4.1 66.7 1.0 N A:CYS447 4.1 81.8 1.0 CA A:CYS446 4.2 86.0 1.0 CA A:CYS447 4.4 81.8 1.0 CA A:GLU371 4.7 82.8 1.0 N A:CYS446 4.8 86.0 1.0 C A:CYS447 4.9 81.8 1.0

Zinc binding site 8 out of 8 in the Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Cryo-Em Structure of Human ZNT1 Wt, in the Presence of Zinc, Determined in An Outward-Facing Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn604 b:109.3 occ:1.00 NE2 A:HIS251 1.9 70.2 1.0 CD2 A:HIS251 2.0 70.2 1.0 OD2 A:ASP255 2.0 75.8 1.0 OD1 A:ASP255 2.0 75.8 1.0 OD1 A:ASP47 2.1 81.3 1.0 CG A:ASP255 2.3 75.8 1.0 CG A:ASP47 2.4 81.3 1.0 OD2 A:ASP47 2.5 81.3 1.0 CE1 A:HIS251 3.2 70.2 1.0 CG A:HIS251 3.3 70.2 1.0 CB A:ASP47 3.5 81.3 1.0 O A:HIS251 3.6 70.2 1.0 CB A:ASP255 3.8 75.8 1.0 ND1 A:HIS251 3.8 70.2 1.0 C A:HIS251 4.1 70.2 1.0 CA A:ASP47 4.2 81.3 1.0 CB A:HIS251 4.4 70.2 1.0 N A:ASP47 4.6 81.3 1.0 CA A:ASP255 4.6 75.8 1.0 N A:ASP255 4.7 75.8 1.0 CA A:HIS251 4.8 70.2 1.0 N A:VAL252 4.8 71.0 1.0 CA A:VAL252 5.0 71.0 1.0

Y.Long, Z.Zhu, Z.Zhou, C.Yang, Y.Chao, Y.Wang, Q.Zhou, M.W.Wang, Q.Qu. Structural Insights Into Human Zinc Transporter ZNT1 Mediated Zn 2+ Efflux. Embo Rep. 2024.
ISSN: ESSN 1469-3178
PubMed: 39390258
DOI: 10.1038/S44319-024-00287-3