Zinc in PDB 8q48: Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng.

All present enzymatic activity of Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng.:
1.6.5.3; 1.6.99.3; 7.1.1.2;

The structure of Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng. also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Iron	(Fe)	28 atoms
Potassium	(K)	1 atom

The binding sites of Zinc atom in the Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng. (pdb code 8q48). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng., PDB code: 8q48:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng. within 5.0Å range: probe atom residue distance (Å) B Occ M:Zn601 b:72.6 occ:1.00 NE2 M:HIS82 2.3 49.6 1.0 NE2 M:HIS338 2.3 52.6 1.0 CE1 M:HIS338 3.1 52.6 1.0 CD2 M:HIS82 3.1 49.6 1.0 O M:GLU335 3.2 51.1 1.0 CD2 M:HIS338 3.3 52.6 1.0 O M:HOH729 3.3 45.2 1.0 CE1 M:HIS82 3.4 49.6 1.0 CA M:GLU335 3.6 51.1 1.0 OD1 g:ASP34 3.6 62.5 1.0 C M:GLU335 3.7 51.1 1.0 CB M:GLU335 3.9 51.1 1.0 ND1 M:HIS338 4.1 52.6 1.0 CG M:GLU335 4.2 51.1 1.0 CG M:HIS338 4.3 52.6 1.0 CG M:HIS82 4.3 49.6 1.0 ND1 M:HIS82 4.4 49.6 1.0 CG g:ASP34 4.5 62.5 1.0 O M:TYR334 4.7 50.0 1.0 N M:GLU335 4.8 51.1 1.0 OD2 g:ASP34 4.9 62.5 1.0 N M:ARG336 5.0 52.9 1.0

Zinc binding site 2 out of 2 in the Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Outward-Facing, Closed Proteoliposome Complex I at 2.5 A. Initially Purified in Lmng. within 5.0Å range: probe atom residue distance (Å) B Occ R:Zn201 b:43.5 occ:1.00 NE2 R:HIS68 2.0 26.7 1.0 SG R:CYS84 2.2 30.6 1.0 SG R:CYS87 2.3 29.2 1.0 SG R:CYS59 2.4 30.2 1.0 CE1 R:HIS68 2.9 26.7 1.0 CD2 R:HIS68 3.1 26.7 1.0 CB R:CYS84 3.3 30.6 1.0 CB R:CYS87 3.4 29.2 1.0 CB R:CYS59 3.5 30.2 1.0 N R:GLY61 3.8 28.4 1.0 N R:CYS87 3.8 29.2 1.0 CA R:GLY61 3.9 28.4 1.0 ND1 R:HIS68 4.0 26.7 1.0 CA R:CYS87 4.2 29.2 1.0 CG R:HIS68 4.2 26.7 1.0 CB R:TYR86 4.4 26.6 1.0 C R:CYS59 4.4 30.2 1.0 O R:CYS59 4.6 30.2 1.0 CA R:CYS59 4.6 30.2 1.0 C R:ASP60 4.7 28.9 1.0 CA R:CYS84 4.7 30.6 1.0 C R:TYR86 4.8 26.6 1.0 N R:ASP60 4.8 28.9 1.0 C R:CYS87 4.8 29.2 1.0 CA R:TYR86 5.0 26.6 1.0 N R:TYR86 5.0 26.6 1.0

D.N.Grba, J.J.Wright, W.Fisher, Z.Yin, J.Hirst. Molecular Mechanism of the Ischemia-Induced Regulatory Switch in Mammalian Complex I Science 2024.
ISSN: ESSN 1095-9203
DOI: 10.1126/SCIENCE.ADO2075