Zinc in PDB 8q47: Inward-Facing, OPEN1 Proteoliposome Complex I at 2.9 A. Initially Purified in Lmng.

All present enzymatic activity of Inward-Facing, OPEN1 Proteoliposome Complex I at 2.9 A. Initially Purified in Lmng.:
1.6.5.3; 1.6.99.3; 7.1.1.2;

The structure of Inward-Facing, OPEN1 Proteoliposome Complex I at 2.9 A. Initially Purified in Lmng. also contains other interesting chemical elements:

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

The binding sites of Zinc atom in the Inward-Facing, OPEN1 Proteoliposome Complex I at 2.9 A. Initially Purified in Lmng. (pdb code 8q47). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Inward-Facing, OPEN1 Proteoliposome Complex I at 2.9 A. Initially Purified in Lmng., PDB code: 8q47:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Inward-Facing, OPEN1 Proteoliposome Complex I at 2.9 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 Inward-Facing, OPEN1 Proteoliposome Complex I at 2.9 A. Initially Purified in Lmng. within 5.0Å range: probe atom residue distance (Å) B Occ M:Zn601 b:78.0 occ:1.00 NE2 M:HIS338 2.3 50.8 1.0 OD2 g:ASP34 2.4 60.0 1.0 O M:GLU335 2.8 47.5 1.0 CE1 M:HIS338 3.0 50.8 1.0 NE2 M:HIS82 3.0 45.9 1.0 CD2 M:HIS338 3.3 50.8 1.0 CG g:ASP34 3.5 60.0 1.0 C M:GLU335 3.7 47.5 1.0 CA M:GLU335 3.9 47.5 1.0 CE1 M:HIS82 4.0 45.9 1.0 CD2 M:HIS82 4.0 45.9 1.0 ND1 M:HIS338 4.1 50.8 1.0 OD1 g:ASP34 4.2 60.0 1.0 CB M:GLU335 4.3 47.5 1.0 CG M:HIS338 4.3 50.8 1.0 CB g:ASP34 4.5 60.0 1.0 CG M:GLU335 4.8 47.5 1.0 N M:ARG336 4.8 47.9 1.0 O M:TYR334 5.0 47.2 1.0

Zinc binding site 2 out of 2 in the Inward-Facing, OPEN1 Proteoliposome Complex I at 2.9 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 Inward-Facing, OPEN1 Proteoliposome Complex I at 2.9 A. Initially Purified in Lmng. within 5.0Å range: probe atom residue distance (Å) B Occ R:Zn201 b:42.9 occ:1.00 NE2 R:HIS68 2.1 30.0 1.0 SG R:CYS87 2.2 32.8 1.0 SG R:CYS84 2.3 34.5 1.0 SG R:CYS59 2.4 33.5 1.0 CE1 R:HIS68 3.0 30.0 1.0 CD2 R:HIS68 3.0 30.0 1.0 CB R:CYS87 3.3 32.8 1.0 CB R:CYS84 3.3 34.5 1.0 CB R:CYS59 3.5 33.5 1.0 N R:CYS87 3.8 32.8 1.0 N R:GLY61 3.9 31.4 1.0 ND1 R:HIS68 4.1 30.0 1.0 CG R:HIS68 4.1 30.0 1.0 CA R:GLY61 4.2 31.4 1.0 CA R:CYS87 4.2 32.8 1.0 C R:CYS59 4.4 33.5 1.0 O R:CYS59 4.4 33.5 1.0 CB R:TYR86 4.5 29.6 1.0 CA R:CYS59 4.5 33.5 1.0 N R:ASP60 4.7 32.1 1.0 C R:ASP60 4.8 32.1 1.0 CA R:CYS84 4.8 34.5 1.0 C R:TYR86 4.8 29.6 1.0 C R:CYS87 4.9 32.8 1.0 N R:TYR86 5.0 29.6 1.0 N R:GLY88 5.0 33.9 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