Magnesium in PDB 8hbf: Structure of Human Soluble Guanylate Cyclase in the No+Rio State at 3.1 Angstrom

All present enzymatic activity of Structure of Human Soluble Guanylate Cyclase in the No+Rio State at 3.1 Angstrom:
4.6.1.2;

The structure of Structure of Human Soluble Guanylate Cyclase in the No+Rio State at 3.1 Angstrom also contains other interesting chemical elements:

Fluorine	(F)	1 atom
Iron	(Fe)	1 atom

The binding sites of Magnesium atom in the Structure of Human Soluble Guanylate Cyclase in the No+Rio State at 3.1 Angstrom (pdb code 8hbf). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Human Soluble Guanylate Cyclase in the No+Rio State at 3.1 Angstrom, PDB code: 8hbf:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Human Soluble Guanylate Cyclase in the No+Rio State at 3.1 Angstrom


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human Soluble Guanylate Cyclase in the No+Rio State at 3.1 Angstrom within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1002 b:37.7 occ:1.00 O5' A:G2P1001 2.0 51.4 1.0 C3A A:G2P1001 2.3 49.2 1.0 PA A:G2P1001 2.4 62.5 1.0 MG A:MG1003 2.5 33.2 1.0 OD2 A:ASP530 2.8 30.8 1.0 OD2 A:ASP486 2.9 41.5 1.0 OD1 A:ASP530 3.0 35.3 1.0 C5' A:G2P1001 3.2 50.6 1.0 O1A A:G2P1001 3.3 56.6 1.0 O3B A:G2P1001 3.3 53.4 1.0 CG A:ASP530 3.3 30.6 1.0 PB A:G2P1001 3.4 57.0 1.0 O2A A:G2P1001 3.7 58.8 1.0 CG A:ASP486 3.8 41.7 1.0 OD1 A:ASP486 4.0 40.3 1.0 C3' A:G2P1001 4.1 58.1 1.0 C4' A:G2P1001 4.2 49.5 1.0 O1B A:G2P1001 4.4 52.9 1.0 O2B A:G2P1001 4.5 50.6 1.0 O A:ILE487 4.7 38.7 1.0 O3' A:G2P1001 4.7 55.8 1.0 CB A:ASP530 4.8 20.1 1.0 PG A:G2P1001 4.8 65.2 1.0

Magnesium binding site 2 out of 2 in the Structure of Human Soluble Guanylate Cyclase in the No+Rio State at 3.1 Angstrom


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Human Soluble Guanylate Cyclase in the No+Rio State at 3.1 Angstrom within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1003 b:33.2 occ:1.00 O3B A:G2P1001 2.0 53.4 1.0 C3A A:G2P1001 2.3 49.2 1.0 PB A:G2P1001 2.3 57.0 1.0 O A:ILE487 2.4 38.7 1.0 MG A:MG1002 2.5 37.7 1.0 OD1 A:ASP486 2.5 40.3 1.0 OD2 A:ASP486 2.6 41.5 1.0 O2B A:G2P1001 2.7 50.6 1.0 OD2 A:ASP530 2.7 30.8 1.0 CG A:ASP486 2.9 41.7 1.0 PG A:G2P1001 3.4 65.2 1.0 O1G A:G2P1001 3.5 49.0 1.0 C A:ILE487 3.6 34.6 1.0 PA A:G2P1001 3.8 62.5 1.0 CG A:ASP530 3.9 30.6 1.0 O1B A:G2P1001 3.9 52.9 1.0 O2G A:G2P1001 3.9 57.1 1.0 N A:ILE487 4.1 38.1 1.0 O5' A:G2P1001 4.2 51.4 1.0 O1A A:G2P1001 4.2 56.6 1.0 CB A:PHE490 4.3 42.3 1.0 OD1 A:ASP530 4.3 35.3 1.0 CB A:ASP486 4.3 30.0 1.0 O3G A:G2P1001 4.4 57.5 1.0 CA A:ILE487 4.4 31.3 1.0 NH2 A:ARG574 4.5 32.6 1.0 N A:VAL488 4.5 35.2 1.0 N A:PHE490 4.6 41.0 1.0 CA A:VAL488 4.6 37.7 1.0 C A:ASP486 4.6 37.1 1.0 N A:GLY489 4.8 47.8 1.0 CA A:ASP486 4.9 28.4 1.0 O2A A:G2P1001 5.0 58.8 1.0 C A:VAL488 5.0 42.7 1.0

R.Liu, Y.Kang, L.Chen. No Binds to the Distal Site of Haem in the Fully Activated Soluble Guanylate Cyclase. Nitric Oxide V.-135 17 2023.
ISSN: ESSN 1089-8611
PubMed: 36972843
DOI: 10.1016/J.NIOX.2023.03.002