Iron in PDB 8gy2: Cryo-Em Structure of Membrane-Bound Alcohol Dehydrogenase From Gluconobacter Oxydans

All present enzymatic activity of Cryo-Em Structure of Membrane-Bound Alcohol Dehydrogenase From Gluconobacter Oxydans:
1.1.5.5;

The structure of Cryo-Em Structure of Membrane-Bound Alcohol Dehydrogenase From Gluconobacter Oxydans also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Iron atom in the Cryo-Em Structure of Membrane-Bound Alcohol Dehydrogenase From Gluconobacter Oxydans (pdb code 8gy2). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Cryo-Em Structure of Membrane-Bound Alcohol Dehydrogenase From Gluconobacter Oxydans, PDB code: 8gy2:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Cryo-Em Structure of Membrane-Bound Alcohol Dehydrogenase From Gluconobacter Oxydans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cryo-Em Structure of Membrane-Bound Alcohol Dehydrogenase From Gluconobacter Oxydans within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:116.4 occ:1.00 FE A:HEC801 0.0 116.4 1.0 NC A:HEC801 2.0 95.2 1.0 NB A:HEC801 2.0 94.9 1.0 NA A:HEC801 2.0 98.1 1.0 ND A:HEC801 2.0 100.7 1.0 NE2 A:HIS657 2.0 85.3 1.0 SD A:MET696 2.8 93.2 1.0 CD2 A:HIS657 2.9 80.1 1.0 C1D A:HEC801 3.0 93.9 1.0 C1B A:HEC801 3.0 91.8 1.0 C4B A:HEC801 3.0 92.9 1.0 C4A A:HEC801 3.0 91.6 1.0 C1C A:HEC801 3.0 88.2 1.0 C4D A:HEC801 3.0 91.2 1.0 C4C A:HEC801 3.0 91.3 1.0 C1A A:HEC801 3.1 86.9 1.0 CE1 A:HIS657 3.1 84.6 1.0 CG A:MET696 3.3 86.1 1.0 CHD A:HEC801 3.4 85.5 1.0 CHB A:HEC801 3.4 88.0 1.0 CHA A:HEC801 3.4 87.4 1.0 CHC A:HEC801 3.4 89.7 1.0 CE A:MET696 3.9 85.5 1.0 CG A:HIS657 4.1 83.0 1.0 ND1 A:HIS657 4.1 85.3 1.0 C3B A:HEC801 4.2 88.7 1.0 C2B A:HEC801 4.2 91.0 1.0 C2D A:HEC801 4.2 87.8 1.0 C3C A:HEC801 4.3 96.2 1.0 C3A A:HEC801 4.3 89.5 1.0 C3D A:HEC801 4.3 87.6 1.0 C2A A:HEC801 4.3 88.1 1.0 C2C A:HEC801 4.3 88.7 1.0 CB A:MET696 4.7 83.2 1.0

Iron binding site 2 out of 4 in the Cryo-Em Structure of Membrane-Bound Alcohol Dehydrogenase From Gluconobacter Oxydans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cryo-Em Structure of Membrane-Bound Alcohol Dehydrogenase From Gluconobacter Oxydans within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:134.6 occ:1.00 FE B:HEC501 0.0 134.6 1.0 NC B:HEC501 2.0 114.6 1.0 NB B:HEC501 2.0 113.5 1.0 NA B:HEC501 2.0 114.5 1.0 ND B:HEC501 2.0 117.0 1.0 NE2 B:HIS60 2.1 108.2 1.0 SD B:MET121 2.8 108.1 1.0 C1D B:HEC501 3.0 111.9 1.0 C1B B:HEC501 3.0 114.1 1.0 C4B B:HEC501 3.0 112.2 1.0 C4A B:HEC501 3.0 114.1 1.0 C1C B:HEC501 3.0 113.2 1.0 C4D B:HEC501 3.0 112.2 1.0 C4C B:HEC501 3.0 110.6 1.0 C1A B:HEC501 3.1 111.4 1.0 CD2 B:HIS60 3.1 109.6 1.0 CE1 B:HIS60 3.1 103.5 1.0 CHD B:HEC501 3.4 108.3 1.0 CHB B:HEC501 3.4 112.8 1.0 CHA B:HEC501 3.4 110.6 1.0 CHC B:HEC501 3.4 112.1 1.0 CG B:MET121 3.5 109.0 1.0 CE B:MET121 4.2 110.5 1.0 C3B B:HEC501 4.2 111.5 1.0 ND1 B:HIS60 4.2 100.8 1.0 C2B B:HEC501 4.2 114.3 1.0 CG B:HIS60 4.2 105.8 1.0 C3C B:HEC501 4.2 116.0 1.0 C2D B:HEC501 4.2 111.1 1.0 C3A B:HEC501 4.3 115.8 1.0 C3D B:HEC501 4.3 112.5 1.0 C2A B:HEC501 4.3 114.3 1.0 C2C B:HEC501 4.3 113.7 1.0 CB B:MET121 4.9 104.7 1.0

Iron binding site 3 out of 4 in the Cryo-Em Structure of Membrane-Bound Alcohol Dehydrogenase From Gluconobacter Oxydans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cryo-Em Structure of Membrane-Bound Alcohol Dehydrogenase From Gluconobacter Oxydans within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe502 b:110.3 occ:1.00 FE B:HEC502 0.0 110.3 1.0 NC B:HEC502 2.0 103.3 1.0 NB B:HEC502 2.0 100.8 1.0 NA B:HEC502 2.0 97.5 1.0 ND B:HEC502 2.0 95.1 1.0 NE2 B:HIS208 2.1 85.4 1.0 SD B:MET277 2.5 92.2 1.0 CE1 B:HIS208 3.0 91.6 1.0 C1D B:HEC502 3.0 91.6 1.0 C1B B:HEC502 3.0 97.0 1.0 C4B B:HEC502 3.0 93.3 1.0 C4A B:HEC502 3.0 98.5 1.0 C1C B:HEC502 3.0 95.6 1.0 C4C B:HEC502 3.1 95.1 1.0 C1A B:HEC502 3.1 93.3 1.0 C4D B:HEC502 3.1 96.1 1.0 CD2 B:HIS208 3.2 82.0 1.0 CHD B:HEC502 3.4 88.4 1.0 CHB B:HEC502 3.4 97.3 1.0 CHA B:HEC502 3.4 92.9 1.0 CHC B:HEC502 3.4 92.6 1.0 CE B:MET277 3.5 86.6 1.0 CG B:MET277 3.7 89.0 1.0 ND1 B:HIS208 4.1 96.6 1.0 C3B B:HEC502 4.2 95.7 1.0 CG B:HIS208 4.2 85.0 1.0 C2B B:HEC502 4.2 92.9 1.0 C2D B:HEC502 4.2 89.5 1.0 C3C B:HEC502 4.3 91.6 1.0 C3A B:HEC502 4.3 95.3 1.0 C2A B:HEC502 4.3 94.5 1.0 C2C B:HEC502 4.3 90.4 1.0 C3D B:HEC502 4.3 91.0 1.0 CB B:MET277 4.4 92.8 1.0 CA B:MET277 5.0 84.3 1.0

Iron binding site 4 out of 4 in the Cryo-Em Structure of Membrane-Bound Alcohol Dehydrogenase From Gluconobacter Oxydans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cryo-Em Structure of Membrane-Bound Alcohol Dehydrogenase From Gluconobacter Oxydans within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe503 b:118.9 occ:1.00 FE B:HEC503 0.0 118.9 1.0 NC B:HEC503 2.0 87.0 1.0 ND B:HEC503 2.0 91.5 1.0 NA B:HEC503 2.0 91.4 1.0 NB B:HEC503 2.0 90.7 1.0 NE2 B:HIS344 2.1 88.3 1.0 SD B:MET394 2.6 82.9 1.0 C1D B:HEC503 3.0 88.6 1.0 C4D B:HEC503 3.0 86.9 1.0 C4C B:HEC503 3.0 89.1 1.0 C1A B:HEC503 3.0 85.1 1.0 C4B B:HEC503 3.0 88.9 1.0 C1B B:HEC503 3.0 83.4 1.0 CD2 B:HIS344 3.1 83.0 1.0 C4A B:HEC503 3.1 86.4 1.0 C1C B:HEC503 3.1 85.1 1.0 CE1 B:HIS344 3.1 79.2 1.0 CHD B:HEC503 3.4 84.8 1.0 CHA B:HEC503 3.4 82.8 1.0 CHB B:HEC503 3.4 86.3 1.0 CE B:MET394 3.4 85.0 1.0 CHC B:HEC503 3.5 89.8 1.0 ND1 B:HIS344 4.2 81.5 1.0 CG B:HIS344 4.2 82.8 1.0 C2D B:HEC503 4.2 90.2 1.0 C3B B:HEC503 4.2 85.7 1.0 C3C B:HEC503 4.2 92.4 1.0 CG B:MET394 4.2 91.8 1.0 C3D B:HEC503 4.3 90.3 1.0 C2B B:HEC503 4.3 82.7 1.0 C2A B:HEC503 4.3 83.2 1.0 C3A B:HEC503 4.3 84.6 1.0 C2C B:HEC503 4.3 87.9 1.0 CB B:MET394 4.9 87.2 1.0

T.Adachi, T.Miyata, F.Makino, H.Tanaka, K.Namba, K.Kano, K.Sowa, Y.Kitazumi, O.Shirai. Experimental and Theoretical Insights Into Bienzymatic Cascade For Mediatorless Bioelectrochemical Ethanol Oxidation with Alcohol and Aldehyde Dehydrogenases Acs Catalysis V. 13 7955 2023.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.3C01962