Zinc in PDB 1h1o: Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer

The structure of Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer, PDB code: 1h1o was solved by C.Abergel, W.Nitschke, G.Malarte, M.Bruschi, J.-M.Claverie, M.-T.Guidici-Orticoni, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25 / 2.13
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	100.049, 100.049, 149.668, 90.00, 90.00, 120.00
R / Rfree (%)	23.9 / 28.4

The structure of Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer also contains other interesting chemical elements:

Iron

(Fe)

4 atoms

The binding sites of Zinc atom in the Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer (pdb code 1h1o). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer, PDB code: 1h1o:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in the Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1187 b:68.4 occ:1.00 O A:HOH2114 2.7 78.4 1.0 O A:HOH2115 3.0 90.4 0.5 NZ A:LYS40 3.5 54.6 1.0 OD1 A:ASN84 3.6 48.3 1.0 ND1 A:HIS39 3.6 43.0 1.0 N A:LYS40 3.8 42.8 1.0 ND2 A:ASN84 3.8 48.8 1.0 CA A:HIS39 3.8 42.7 1.0 CB A:HIS39 3.9 43.0 1.0 CG A:ASN84 4.0 49.3 1.0 CG A:HIS39 4.2 43.2 1.0 CE A:LYS40 4.2 51.3 1.0 C A:HIS39 4.3 42.8 1.0 CG A:LYS40 4.4 47.4 1.0 CB A:LYS40 4.6 44.2 1.0 O A:HOH2001 4.6 54.5 1.0 CE1 A:HIS39 4.7 44.6 1.0 CA A:LYS40 4.8 43.4 1.0 CD A:LYS40 5.0 51.1 1.0

Zinc binding site 2 out of 6 in the Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1188 b:65.3 occ:1.00 O A:HOH2084 3.3 37.7 1.0 N A:TYR141 3.7 35.6 1.0 OG A:SER93 3.7 60.7 1.0 NE2 A:HIS97 3.7 46.3 1.0 NH2 A:ARG34 3.7 34.5 1.0 NE A:ARG140 4.0 38.3 1.0 NH2 A:ARG140 4.0 35.9 1.0 CB A:TYR141 4.1 36.0 1.0 CD1 A:ILE95 4.1 63.4 1.0 CA A:ARG140 4.2 35.0 1.0 CB A:ARG140 4.4 34.7 1.0 C A:ARG140 4.5 35.7 1.0 CZ A:ARG140 4.5 37.8 1.0 CD2 A:HIS97 4.5 45.8 1.0 CB A:SER93 4.5 59.7 1.0 CA A:TYR141 4.6 36.0 1.0 CZ A:ARG34 4.6 36.6 1.0 NH1 A:ARG34 4.6 36.9 1.0 CE1 A:HIS97 4.7 47.3 1.0 CB A:ILE95 4.8 60.6 1.0 CG1 A:ILE95 4.8 62.6 1.0 CG A:ARG140 4.9 36.0 1.0 CB A:SER181 5.0 38.2 1.0

Zinc binding site 3 out of 6 in the Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1189 b:100.0 occ:1.00 NE2 A:HIS152 2.3 35.1 1.0 CD2 A:HIS152 3.2 33.4 1.0 CE1 A:HIS152 3.3 34.8 1.0 O A:HOH2103 3.7 68.9 1.0 CG A:HIS152 4.4 35.6 1.0 ND1 A:HIS152 4.4 35.9 1.0 O A:HOH2091 4.4 62.4 1.0 O A:HOH2104 4.7 57.7 1.0

Zinc binding site 4 out of 6 in the Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1388 b:36.3 occ:1.00 ND1 B:HIS239 2.1 29.4 1.0 OE1 A:GLU121 2.2 34.9 1.0 O1 B:SO41387 2.2 32.8 1.0 O B:HOH2068 2.4 35.9 1.0 O4 B:SO41387 2.6 32.8 1.0 OE2 A:GLU121 2.6 30.4 1.0 CD A:GLU121 2.7 30.7 1.0 S B:SO41387 2.9 35.6 1.0 CE1 B:HIS239 3.0 29.0 1.0 CG B:HIS239 3.1 29.6 1.0 CB B:HIS239 3.4 32.5 1.0 CA B:HIS239 3.6 34.6 1.0 ND2 B:ASN284 3.8 38.0 1.0 O3 B:SO41387 3.9 34.4 1.0 O2 B:SO41387 4.0 33.8 1.0 O A:HOH2075 4.1 43.2 1.0 NE2 B:HIS239 4.1 29.7 1.0 CD2 B:HIS239 4.2 29.6 1.0 CG A:GLU121 4.2 32.2 1.0 N B:GLY331 4.4 32.5 1.0 N B:LYS240 4.5 36.5 1.0 N B:HIS239 4.6 34.0 1.0 O B:HOH2067 4.6 33.3 1.0 C B:HIS239 4.6 35.9 1.0 O B:HOH2044 4.8 41.2 1.0 CA B:ALA330 4.9 34.2 1.0 CG B:ASN284 5.0 40.3 1.0

Zinc binding site 5 out of 6 in the Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1389 b:96.4 occ:1.00 NE2 B:HIS352 2.3 55.3 1.0 O B:HOH2069 3.0 66.0 1.0 CD2 B:HIS352 3.1 54.0 1.0 O B:HOH2070 3.3 71.5 1.0 CE1 B:HIS352 3.3 54.9 1.0 CG B:HIS352 4.3 52.8 1.0 ND1 B:HIS352 4.3 54.5 1.0 O B:HOH2009 4.4 60.8 1.0 O B:HOH2071 4.4 64.1 1.0

Zinc binding site 6 out of 6 in the Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Acidithiobacillus Ferrooxidans Cytochrome C4 Structure Supports A Complex-Induced Tuning of Electron Transfer within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1390 b:79.0 occ:1.00 O B:HOH2049 3.3 50.5 1.0 NH1 B:ARG234 3.5 40.5 1.0 NE2 B:HIS297 3.6 68.8 1.0 CD B:ARG340 3.8 44.6 1.0 N B:TYR341 4.0 38.5 1.0 NH1 B:ARG340 4.2 45.1 1.0 NH2 B:ARG234 4.2 42.5 1.0 CA B:ARG340 4.2 38.1 1.0 CZ B:ARG234 4.3 41.6 1.0 O B:HOH2035 4.3 57.4 1.0 CD2 B:HIS297 4.3 69.1 1.0 NZ B:LYS296 4.4 79.3 1.0 CB B:TYR341 4.4 41.0 1.0 O B:SER292 4.5 69.3 1.0 CB B:ARG340 4.6 38.4 1.0 CE1 B:HIS297 4.6 68.7 1.0 C B:ARG340 4.7 37.8 1.0 CG B:ARG340 4.8 40.4 1.0 NE B:ARG340 4.9 46.0 1.0 CA B:TYR341 4.9 40.0 1.0 CB B:SER381 4.9 42.8 1.0

C.Abergel, W.Nitschke, G.Malarte, M.Bruschi, J.-M.Claverie, M.-T.Guidici-Orticoni. The Structure of Acidithiobacillus Ferrooxidans C(4)-Cytochrome. A Model For Complex-Induced Electron Transfer Tuning Structure V. 11 547 2003.
ISSN: ISSN 0969-2126
PubMed: 12737820
DOI: 10.1016/S0969-2126(03)00072-8