Calcium in PDB 6o77: Structure of the TRPM8 Cold Receptor By Single Particle Electron Cryo- Microscopy, Calcium-Bound State

The binding sites of Calcium atom in the Structure of the TRPM8 Cold Receptor By Single Particle Electron Cryo- Microscopy, Calcium-Bound State (pdb code 6o77). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the Structure of the TRPM8 Cold Receptor By Single Particle Electron Cryo- Microscopy, Calcium-Bound State, PDB code: 6o77:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the Structure of the TRPM8 Cold Receptor By Single Particle Electron Cryo- Microscopy, Calcium-Bound State


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of the TRPM8 Cold Receptor By Single Particle Electron Cryo- Microscopy, Calcium-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1401 b:1.0 occ:1.00 OD1 A:ASN790 2.5 0.3 1.0 OE2 A:GLU773 2.5 0.1 1.0 OE1 A:GLN776 2.6 0.5 1.0 NE2 A:GLN776 2.6 0.5 1.0 CD A:GLN776 2.9 0.5 1.0 OD2 A:ASP793 3.0 93.3 1.0 CD A:GLU773 3.5 0.1 1.0 CG A:ASN790 3.6 0.3 1.0 OE1 A:GLU773 3.7 0.1 1.0 ND2 A:ASN790 4.1 0.3 1.0 CG A:ASP793 4.2 93.3 1.0 CG A:GLN776 4.4 0.5 1.0 NH2 A:ARG832 4.8 68.9 1.0 CG A:GLU773 4.9 0.1 1.0 OD1 A:ASP793 4.9 93.3 1.0 CB A:ASN790 4.9 0.3 1.0

Calcium binding site 2 out of 4 in the Structure of the TRPM8 Cold Receptor By Single Particle Electron Cryo- Microscopy, Calcium-Bound State


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of the TRPM8 Cold Receptor By Single Particle Electron Cryo- Microscopy, Calcium-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1401 b:1.0 occ:1.00 OD1 B:ASN790 2.5 0.3 1.0 OE2 B:GLU773 2.5 0.1 1.0 OE1 B:GLN776 2.6 0.5 1.0 NE2 B:GLN776 2.6 0.5 1.0 CD B:GLN776 2.9 0.5 1.0 OD2 B:ASP793 3.0 93.3 1.0 CD B:GLU773 3.5 0.1 1.0 CG B:ASN790 3.6 0.3 1.0 OE1 B:GLU773 3.7 0.1 1.0 ND2 B:ASN790 4.1 0.3 1.0 CG B:ASP793 4.2 93.3 1.0 CG B:GLN776 4.4 0.5 1.0 NH2 B:ARG832 4.8 68.9 1.0 CG B:GLU773 4.9 0.1 1.0 OD1 B:ASP793 4.9 93.3 1.0 CB B:ASN790 4.9 0.3 1.0

Calcium binding site 3 out of 4 in the Structure of the TRPM8 Cold Receptor By Single Particle Electron Cryo- Microscopy, Calcium-Bound State


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Structure of the TRPM8 Cold Receptor By Single Particle Electron Cryo- Microscopy, Calcium-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca1401 b:1.0 occ:1.00 OD1 C:ASN790 2.5 0.3 1.0 OE2 C:GLU773 2.5 0.1 1.0 OE1 C:GLN776 2.6 0.5 1.0 NE2 C:GLN776 2.6 0.5 1.0 CD C:GLN776 2.9 0.5 1.0 OD2 C:ASP793 3.0 93.3 1.0 CD C:GLU773 3.5 0.1 1.0 CG C:ASN790 3.6 0.3 1.0 OE1 C:GLU773 3.7 0.1 1.0 ND2 C:ASN790 4.1 0.3 1.0 CG C:ASP793 4.2 93.3 1.0 CG C:GLN776 4.4 0.5 1.0 NH2 C:ARG832 4.8 68.9 1.0 CG C:GLU773 4.9 0.1 1.0 OD1 C:ASP793 4.9 93.3 1.0 CB C:ASN790 4.9 0.3 1.0

Calcium binding site 4 out of 4 in the Structure of the TRPM8 Cold Receptor By Single Particle Electron Cryo- Microscopy, Calcium-Bound State


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Structure of the TRPM8 Cold Receptor By Single Particle Electron Cryo- Microscopy, Calcium-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca1401 b:1.0 occ:1.00 OD1 D:ASN790 2.5 0.3 1.0 OE2 D:GLU773 2.5 0.1 1.0 OE1 D:GLN776 2.6 0.5 1.0 NE2 D:GLN776 2.6 0.5 1.0 CD D:GLN776 2.9 0.5 1.0 OD2 D:ASP793 3.0 93.3 1.0 CD D:GLU773 3.5 0.1 1.0 CG D:ASN790 3.6 0.3 1.0 OE1 D:GLU773 3.7 0.1 1.0 ND2 D:ASN790 4.1 0.3 1.0 CG D:ASP793 4.2 93.3 1.0 CG D:GLN776 4.4 0.5 1.0 NH2 D:ARG832 4.8 68.9 1.0 CG D:GLU773 4.9 0.1 1.0 OD1 D:ASP793 4.9 93.3 1.0 CB D:ASN790 4.9 0.3 1.0

M.M.Diver, Y.Cheng, D.Julius. Structural Insights Into TRPM8 Inhibition and Desensitization. Science V. 365 1434 2019.
ISSN: ESSN 1095-9203
PubMed: 31488702
DOI: 10.1126/SCIENCE.AAX6672