Magnesium in PDB 3j7h: Structure of Beta-Galactosidase at 3.2-A Resolution Obtained By Cryo- Electron Microscopy

All present enzymatic activity of Structure of Beta-Galactosidase at 3.2-A Resolution Obtained By Cryo- Electron Microscopy:
3.2.1.23;

The binding sites of Magnesium atom in the Structure of Beta-Galactosidase at 3.2-A Resolution Obtained By Cryo- Electron Microscopy (pdb code 3j7h). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Structure of Beta-Galactosidase at 3.2-A Resolution Obtained By Cryo- Electron Microscopy, PDB code: 3j7h:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Structure of Beta-Galactosidase at 3.2-A Resolution Obtained By Cryo- Electron Microscopy


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Beta-Galactosidase at 3.2-A Resolution Obtained By Cryo- Electron Microscopy within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg3001 b:16.1 occ:1.00 ND1 A:HIS418 1.5 11.4 1.0 OE2 A:GLU416 1.6 11.7 1.0 OE1 A:GLU461 1.7 13.9 1.0 CE1 A:HIS418 2.4 12.3 1.0 CG A:HIS418 2.6 15.0 1.0 CD A:GLU416 2.8 15.4 1.0 CD A:GLU461 3.0 19.5 1.0 CB A:HIS418 3.2 13.0 1.0 NE2 A:HIS418 3.5 11.3 1.0 CD2 A:HIS418 3.6 12.0 1.0 OE1 A:GLU416 3.7 11.8 1.0 OE2 A:GLU461 3.8 13.7 1.0 CG A:GLU416 3.8 8.0 1.0 CB A:GLU461 3.8 10.0 1.0 CG A:GLU461 4.0 9.5 1.0 O A:ASP199 4.2 15.8 1.0 O A:ASN102 4.3 13.8 1.0 CA A:GLN200 4.3 7.8 1.0 N A:ASP201 4.4 10.8 1.0 CA A:HIS418 4.4 12.2 1.0 C A:ASP199 4.7 15.3 1.0 N A:HIS418 4.7 13.6 1.0 CG A:ASP201 4.8 17.0 1.0 C A:GLN200 4.8 12.7 1.0 OD2 A:ASP201 4.9 11.7 1.0 N A:GLN200 4.9 9.2 1.0

Magnesium binding site 2 out of 4 in the Structure of Beta-Galactosidase at 3.2-A Resolution Obtained By Cryo- Electron Microscopy


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Beta-Galactosidase at 3.2-A Resolution Obtained By Cryo- Electron Microscopy within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg3001 b:16.1 occ:1.00 ND1 B:HIS418 1.5 11.4 1.0 OE2 B:GLU416 1.6 11.7 1.0 OE1 B:GLU461 1.7 13.9 1.0 CE1 B:HIS418 2.4 12.3 1.0 CG B:HIS418 2.6 15.0 1.0 CD B:GLU416 2.8 15.4 1.0 CD B:GLU461 3.0 19.5 1.0 CB B:HIS418 3.2 13.0 1.0 NE2 B:HIS418 3.5 11.3 1.0 CD2 B:HIS418 3.6 12.0 1.0 OE1 B:GLU416 3.7 11.8 1.0 OE2 B:GLU461 3.8 13.7 1.0 CG B:GLU416 3.8 8.0 1.0 CB B:GLU461 3.8 10.0 1.0 CG B:GLU461 4.0 9.5 1.0 O B:ASP199 4.2 15.8 1.0 O B:ASN102 4.3 13.8 1.0 CA B:GLN200 4.3 7.8 1.0 N B:ASP201 4.4 10.8 1.0 CA B:HIS418 4.4 12.2 1.0 C B:ASP199 4.7 15.3 1.0 N B:HIS418 4.7 13.6 1.0 CG B:ASP201 4.8 17.0 1.0 C B:GLN200 4.8 12.7 1.0 OD2 B:ASP201 4.9 11.7 1.0 N B:GLN200 4.9 9.2 1.0

Magnesium binding site 3 out of 4 in the Structure of Beta-Galactosidase at 3.2-A Resolution Obtained By Cryo- Electron Microscopy


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of Beta-Galactosidase at 3.2-A Resolution Obtained By Cryo- Electron Microscopy within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg3001 b:16.1 occ:1.00 ND1 C:HIS418 1.5 11.4 1.0 OE2 C:GLU416 1.6 11.7 1.0 OE1 C:GLU461 1.7 13.9 1.0 CE1 C:HIS418 2.4 12.3 1.0 CG C:HIS418 2.6 15.0 1.0 CD C:GLU416 2.8 15.4 1.0 CD C:GLU461 3.0 19.5 1.0 CB C:HIS418 3.2 13.0 1.0 NE2 C:HIS418 3.5 11.3 1.0 CD2 C:HIS418 3.6 12.0 1.0 OE1 C:GLU416 3.7 11.8 1.0 OE2 C:GLU461 3.8 13.7 1.0 CG C:GLU416 3.8 8.0 1.0 CB C:GLU461 3.8 10.0 1.0 CG C:GLU461 4.0 9.5 1.0 O C:ASP199 4.2 15.8 1.0 O C:ASN102 4.3 13.8 1.0 CA C:GLN200 4.3 7.8 1.0 N C:ASP201 4.4 10.8 1.0 CA C:HIS418 4.4 12.2 1.0 C C:ASP199 4.7 15.3 1.0 N C:HIS418 4.7 13.6 1.0 CG C:ASP201 4.8 17.0 1.0 C C:GLN200 4.8 12.7 1.0 OD2 C:ASP201 4.9 11.7 1.0 N C:GLN200 4.9 9.2 1.0

Magnesium binding site 4 out of 4 in the Structure of Beta-Galactosidase at 3.2-A Resolution Obtained By Cryo- Electron Microscopy


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structure of Beta-Galactosidase at 3.2-A Resolution Obtained By Cryo- Electron Microscopy within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg3001 b:16.1 occ:1.00 ND1 D:HIS418 1.5 11.4 1.0 OE2 D:GLU416 1.6 11.7 1.0 OE1 D:GLU461 1.7 13.9 1.0 CE1 D:HIS418 2.4 12.3 1.0 CG D:HIS418 2.6 15.0 1.0 CD D:GLU416 2.8 15.4 1.0 CD D:GLU461 3.0 19.5 1.0 CB D:HIS418 3.2 13.0 1.0 NE2 D:HIS418 3.5 11.3 1.0 CD2 D:HIS418 3.6 12.0 1.0 OE1 D:GLU416 3.7 11.8 1.0 OE2 D:GLU461 3.8 13.7 1.0 CG D:GLU416 3.8 8.0 1.0 CB D:GLU461 3.8 10.0 1.0 CG D:GLU461 4.0 9.5 1.0 O D:ASP199 4.2 15.8 1.0 O D:ASN102 4.3 13.8 1.0 CA D:GLN200 4.3 7.8 1.0 N D:ASP201 4.4 10.8 1.0 CA D:HIS418 4.4 12.2 1.0 C D:ASP199 4.7 15.3 1.0 N D:HIS418 4.7 13.6 1.0 CG D:ASP201 4.8 17.0 1.0 C D:GLN200 4.8 12.7 1.0 OD2 D:ASP201 4.9 11.7 1.0 N D:GLN200 4.9 9.2 1.0

A.Bartesaghi, D.Matthies, S.Banerjee, A.Merk, S.Subramaniam. Structure of Beta-Galactosidase at 3.2- Angstrom Resolution Obtained By Cryo-Electron Microscopy. Proc.Natl.Acad.Sci.Usa V. 111 11709 2014.
ISSN: ISSN 0027-8424
PubMed: 25071206
DOI: 10.1073/PNAS.1402809111