Zinc in PDB 6u9w: Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Atp-Bound, Open State

The binding sites of Zinc atom in the Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Atp-Bound, Open State (pdb code 6u9w). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Atp-Bound, Open State, PDB code: 6u9w:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in the Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Atp-Bound, Open State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Atp-Bound, Open State within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:78.5 occ:1.00 SG A:CYS506 2.3 57.7 1.0 SG A:CYS499 2.3 54.3 1.0 SG A:CYS572 2.4 52.3 1.0 SG A:CYS479 2.4 61.3 1.0 HB2 A:CYS479 2.5 61.3 1.0 CB A:CYS479 2.9 61.3 1.0 HB3 A:CYS479 3.1 61.3 1.0 HB3 A:CYS572 3.2 52.3 1.0 CB A:CYS572 3.3 52.3 1.0 HB2 A:CYS572 3.4 52.3 1.0 H A:CYS499 3.5 54.3 1.0 HB3 A:CYS499 3.6 54.3 1.0 HB2 A:ASN481 3.6 60.1 1.0 CB A:CYS499 3.7 54.3 1.0 CB A:CYS506 3.7 57.7 1.0 HB2 A:CYS506 3.8 57.7 1.0 HA A:CYS506 3.8 57.7 1.0 H A:ILE507 3.9 53.2 1.0 ZN A:ZN702 4.1 89.0 1.0 CA A:CYS506 4.3 57.7 1.0 HB2 A:CYS499 4.3 54.3 1.0 N A:CYS499 4.3 54.3 1.0 CA A:CYS479 4.3 61.3 1.0 H A:ASN481 4.4 60.1 1.0 HB3 A:CYS506 4.5 57.7 1.0 HG22 A:THR508 4.5 53.4 1.0 CB A:ASN481 4.6 60.1 1.0 OD1 A:ASN481 4.6 60.1 1.0 H A:CYS572 4.6 52.3 1.0 N A:ILE507 4.6 53.2 1.0 CA A:CYS499 4.6 54.3 1.0 H A:THR508 4.6 53.4 1.0 HA A:CYS479 4.7 61.3 1.0 SG A:CYS498 4.7 52.2 1.0 CA A:CYS572 4.7 52.3 1.0 SG A:CYS482 4.8 58.0 1.0 C A:CYS479 4.8 61.3 1.0 H A:ARG500 4.8 58.5 1.0 O A:CYS479 4.9 61.3 1.0 HA A:CYS498 5.0 52.2 1.0 HB2 A:PRO570 5.0 47.4 1.0

Zinc binding site 2 out of 6 in the Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Atp-Bound, Open State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Atp-Bound, Open State within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn702 b:89.0 occ:1.00 SG A:CYS477 2.3 60.3 1.0 H A:CYS479 2.3 61.3 1.0 SG A:CYS482 2.3 58.0 1.0 SG A:CYS479 2.3 61.3 1.0 SG A:CYS498 2.3 52.2 1.0 HB3 A:CYS479 2.4 61.3 1.0 HB2 A:CYS477 2.4 60.3 1.0 CB A:CYS479 2.7 61.3 1.0 CB A:CYS477 2.7 60.3 1.0 N A:CYS479 3.0 61.3 1.0 H A:CYS482 3.1 58.0 1.0 H A:GLY480 3.2 60.9 1.0 HA A:CYS477 3.2 60.3 1.0 CA A:CYS479 3.3 61.3 1.0 H A:ASN481 3.4 60.1 1.0 CA A:CYS477 3.5 60.3 1.0 HB2 A:CYS482 3.5 58.0 1.0 CB A:CYS482 3.5 58.0 1.0 HB2 A:CYS479 3.6 61.3 1.0 HB3 A:CYS477 3.6 60.3 1.0 CB A:CYS498 3.6 52.2 1.0 N A:GLY480 3.6 60.9 1.0 HB2 A:CYS498 3.7 52.2 1.0 HA A:CYS498 3.7 52.2 1.0 N A:CYS482 3.8 58.0 1.0 C A:CYS479 3.8 61.3 1.0 C A:CYS477 3.8 60.3 1.0 H A:GLN478 3.9 60.4 1.0 N A:GLN478 3.9 60.4 1.0 H A:CYS499 4.0 54.3 1.0 ZN A:ZN701 4.1 78.5 1.0 HA A:CYS479 4.2 61.3 1.0 N A:ASN481 4.2 60.1 1.0 CA A:CYS482 4.2 58.0 1.0 CA A:CYS498 4.2 52.2 1.0 C A:GLN478 4.3 60.4 1.0 HB3 A:CYS482 4.3 58.0 1.0 HB3 A:CYS498 4.4 52.2 1.0 HA A:CYS482 4.5 58.0 1.0 HB3 A:CYS572 4.5 52.3 1.0 O A:CYS477 4.6 60.3 1.0 C A:ASN481 4.7 60.1 1.0 CA A:GLY480 4.7 60.9 1.0 CA A:GLN478 4.7 60.4 1.0 O A:CYS479 4.8 61.3 1.0 N A:CYS499 4.8 54.3 1.0 N A:CYS477 4.8 60.3 1.0 C A:GLY480 4.9 60.9 1.0 SG A:CYS499 4.9 54.3 1.0 HB2 A:ASN481 4.9 60.1 1.0 O A:LEU497 5.0 49.1 1.0 CA A:ASN481 5.0 60.1 1.0

Zinc binding site 3 out of 6 in the Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Atp-Bound, Open State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Atp-Bound, Open State within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn701 b:81.3 occ:1.00 SG B:CYS506 2.3 57.3 1.0 SG B:CYS499 2.3 53.6 1.0 SG B:CYS572 2.4 52.1 1.0 SG B:CYS479 2.4 60.2 1.0 HB2 B:CYS479 2.6 60.2 1.0 CB B:CYS479 2.9 60.2 1.0 HB3 B:CYS479 3.1 60.2 1.0 HB3 B:CYS572 3.2 52.1 1.0 CB B:CYS572 3.3 52.1 1.0 HB3 B:CYS499 3.4 53.6 1.0 HB2 B:CYS572 3.4 52.1 1.0 H B:CYS499 3.4 53.6 1.0 CB B:CYS499 3.5 53.6 1.0 HB2 B:ASN481 3.6 58.6 1.0 CB B:CYS506 3.6 57.3 1.0 HB2 B:CYS506 3.7 57.3 1.0 HA B:CYS506 3.7 57.3 1.0 H B:ILE507 3.8 53.2 1.0 ZN B:ZN702 4.1 86.3 1.0 HB2 B:CYS499 4.2 53.6 1.0 N B:CYS499 4.2 53.6 1.0 CA B:CYS506 4.2 57.3 1.0 CA B:CYS479 4.4 60.2 1.0 H B:ASN481 4.4 58.6 1.0 HB3 B:CYS506 4.4 57.3 1.0 OD1 B:ASN481 4.5 58.6 1.0 CB B:ASN481 4.5 58.6 1.0 CA B:CYS499 4.5 53.6 1.0 HG22 B:THR508 4.6 54.2 1.0 H B:CYS572 4.6 52.1 1.0 N B:ILE507 4.6 53.2 1.0 SG B:CYS498 4.6 51.5 1.0 SG B:CYS482 4.7 56.6 1.0 HA B:CYS479 4.7 60.2 1.0 CA B:CYS572 4.7 52.1 1.0 H B:ARG500 4.7 56.4 1.0 H B:THR508 4.7 54.2 1.0 C B:CYS479 4.8 60.2 1.0 O B:CYS479 4.9 60.2 1.0 C B:CYS506 5.0 57.3 1.0 HA B:CYS498 5.0 51.5 1.0 HB3 B:ASN481 5.0 58.6 1.0

Zinc binding site 4 out of 6 in the Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Atp-Bound, Open State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Atp-Bound, Open State within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn702 b:86.3 occ:1.00 HB2 B:CYS477 2.1 58.7 1.0 SG B:CYS477 2.3 58.7 1.0 SG B:CYS482 2.3 56.6 1.0 SG B:CYS479 2.3 60.2 1.0 HB3 B:CYS479 2.4 60.2 1.0 SG B:CYS498 2.4 51.5 1.0 H B:CYS479 2.4 60.2 1.0 CB B:CYS477 2.5 58.7 1.0 CB B:CYS479 2.7 60.2 1.0 N B:CYS479 3.1 60.2 1.0 H B:CYS482 3.1 56.6 1.0 HA B:CYS477 3.3 58.7 1.0 CA B:CYS479 3.3 60.2 1.0 H B:GLY480 3.3 60.4 1.0 HB3 B:CYS477 3.3 58.7 1.0 CA B:CYS477 3.4 58.7 1.0 HB2 B:CYS482 3.4 56.6 1.0 H B:ASN481 3.4 58.6 1.0 CB B:CYS482 3.5 56.6 1.0 HB2 B:CYS479 3.6 60.2 1.0 CB B:CYS498 3.7 51.5 1.0 HA B:CYS498 3.7 51.5 1.0 N B:GLY480 3.7 60.4 1.0 HB2 B:CYS498 3.7 51.5 1.0 N B:CYS482 3.8 56.6 1.0 C B:CYS477 3.8 58.7 1.0 C B:CYS479 3.8 60.2 1.0 H B:GLN478 3.9 58.6 1.0 N B:GLN478 3.9 58.6 1.0 H B:CYS499 4.0 53.6 1.0 ZN B:ZN701 4.1 81.3 1.0 HA B:CYS479 4.2 60.2 1.0 CA B:CYS482 4.2 56.6 1.0 N B:ASN481 4.2 58.6 1.0 CA B:CYS498 4.2 51.5 1.0 HB3 B:CYS482 4.3 56.6 1.0 C B:GLN478 4.3 58.6 1.0 HB3 B:CYS498 4.5 51.5 1.0 HA B:CYS482 4.5 56.6 1.0 O B:CYS477 4.6 58.7 1.0 HB3 B:CYS572 4.6 52.1 1.0 N B:CYS499 4.7 53.6 1.0 C B:ASN481 4.8 58.6 1.0 CA B:GLN478 4.8 58.6 1.0 N B:CYS477 4.8 58.7 1.0 O B:CYS479 4.8 60.2 1.0 CA B:GLY480 4.8 60.4 1.0 O B:LEU497 4.9 48.8 1.0 SG B:CYS499 4.9 53.6 1.0 HB2 B:ASN481 4.9 58.6 1.0 C B:GLY480 5.0 60.4 1.0

Zinc binding site 5 out of 6 in the Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Atp-Bound, Open State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Atp-Bound, Open State within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn702 b:78.7 occ:1.00 SG C:CYS506 2.3 58.2 1.0 SG C:CYS499 2.3 53.2 1.0 SG C:CYS572 2.4 53.4 1.0 SG C:CYS479 2.4 61.2 1.0 HB2 C:CYS479 2.5 61.2 1.0 CB C:CYS479 2.8 61.2 1.0 HB3 C:CYS479 3.0 61.2 1.0 HB3 C:CYS572 3.1 53.4 1.0 CB C:CYS572 3.2 53.4 1.0 HB2 C:CYS572 3.4 53.4 1.0 H C:CYS499 3.5 53.2 1.0 HB3 C:CYS499 3.6 53.2 1.0 HB2 C:ASN481 3.6 60.9 1.0 CB C:CYS499 3.6 53.2 1.0 CB C:CYS506 3.7 58.2 1.0 HB2 C:CYS506 3.8 58.2 1.0 HA C:CYS506 3.8 58.2 1.0 H C:ILE507 3.8 53.6 1.0 ZN C:ZN703 4.1 88.7 1.0 HB2 C:CYS499 4.3 53.2 1.0 CA C:CYS479 4.3 61.2 1.0 N C:CYS499 4.3 53.2 1.0 CA C:CYS506 4.3 58.2 1.0 H C:ASN481 4.4 60.9 1.0 HG C:CYS573 4.4 50.6 1.0 HB3 C:CYS506 4.5 58.2 1.0 HG22 C:THR508 4.5 54.3 1.0 OD1 C:ASN481 4.5 60.9 1.0 H C:CYS572 4.6 53.4 1.0 CB C:ASN481 4.6 60.9 1.0 N C:ILE507 4.6 53.6 1.0 CA C:CYS499 4.6 53.2 1.0 HA C:CYS479 4.6 61.2 1.0 SG C:CYS498 4.6 51.5 1.0 H C:THR508 4.7 54.3 1.0 CA C:CYS572 4.7 53.4 1.0 H C:ARG500 4.8 57.4 1.0 C C:CYS479 4.8 61.2 1.0 SG C:CYS482 4.8 59.6 1.0 O C:CYS479 4.9 61.2 1.0 HA C:CYS498 5.0 51.5 1.0

Zinc binding site 6 out of 6 in the Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Atp-Bound, Open State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Atp-Bound, Open State within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn703 b:88.7 occ:1.00 H C:CYS479 2.3 61.2 1.0 SG C:CYS477 2.3 62.8 1.0 SG C:CYS482 2.3 59.6 1.0 SG C:CYS479 2.3 61.2 1.0 SG C:CYS498 2.4 51.5 1.0 HB2 C:CYS477 2.4 62.8 1.0 HB3 C:CYS479 2.4 61.2 1.0 CB C:CYS479 2.7 61.2 1.0 CB C:CYS477 2.7 62.8 1.0 N C:CYS479 3.0 61.2 1.0 H C:CYS482 3.1 59.6 1.0 HA C:CYS477 3.2 62.8 1.0 H C:GLY480 3.2 62.0 1.0 CA C:CYS479 3.3 61.2 1.0 H C:ASN481 3.4 60.9 1.0 CA C:CYS477 3.4 62.8 1.0 HB2 C:CYS482 3.5 59.6 1.0 CB C:CYS482 3.5 59.6 1.0 HB3 C:CYS477 3.6 62.8 1.0 HB2 C:CYS479 3.6 61.2 1.0 N C:GLY480 3.6 62.0 1.0 CB C:CYS498 3.7 51.5 1.0 HB2 C:CYS498 3.7 51.5 1.0 HA C:CYS498 3.7 51.5 1.0 N C:CYS482 3.8 59.6 1.0 C C:CYS479 3.8 61.2 1.0 C C:CYS477 3.8 62.8 1.0 H C:GLN478 3.8 60.4 1.0 N C:GLN478 3.9 60.4 1.0 ZN C:ZN702 4.1 78.7 1.0 H C:CYS499 4.1 53.2 1.0 N C:ASN481 4.2 60.9 1.0 HA C:CYS479 4.2 61.2 1.0 CA C:CYS482 4.2 59.6 1.0 C C:GLN478 4.2 60.4 1.0 CA C:CYS498 4.3 51.5 1.0 HB3 C:CYS482 4.3 59.6 1.0 HB3 C:CYS498 4.4 51.5 1.0 HB3 C:CYS572 4.5 53.4 1.0 HA C:CYS482 4.5 59.6 1.0 O C:CYS477 4.6 62.8 1.0 CA C:GLN478 4.7 60.4 1.0 C C:ASN481 4.7 60.9 1.0 CA C:GLY480 4.8 62.0 1.0 O C:CYS479 4.8 61.2 1.0 N C:CYS499 4.8 53.2 1.0 N C:CYS477 4.8 62.8 1.0 SG C:CYS499 4.9 53.2 1.0 C C:GLY480 4.9 62.0 1.0 HB2 C:ASN481 4.9 60.9 1.0 CA C:ASN481 5.0 60.9 1.0 O C:LEU497 5.0 49.9 1.0

A.E.Mccarthy, C.Yoshioka, S.E.Mansoor. Full-Length P2X7STRUCTURES Reveal How Palmitoylation Prevents Channel Desensitization. Cell V. 179 659 2019.
ISSN: ISSN 1097-4172
PubMed: 31587896
DOI: 10.1016/J.CELL.2019.09.017