Atomistry » Zinc » PDB 7b8e-7bos » 7bkb
Atomistry »
  Zinc »
    PDB 7b8e-7bos »
      7bkb »

Zinc in PDB 7bkb: Formate Dehydrogenase - Heterodisulfide Reductase - Formylmethanofuran Dehydrogenase Complex From Methanospirillum Hungatei (Hexameric, Composite Structure)

Enzymatic activity of Formate Dehydrogenase - Heterodisulfide Reductase - Formylmethanofuran Dehydrogenase Complex From Methanospirillum Hungatei (Hexameric, Composite Structure)

All present enzymatic activity of Formate Dehydrogenase - Heterodisulfide Reductase - Formylmethanofuran Dehydrogenase Complex From Methanospirillum Hungatei (Hexameric, Composite Structure):
1.17.1.9; 1.2.7.12; 1.2.99.5;

Other elements in 7bkb:

The structure of Formate Dehydrogenase - Heterodisulfide Reductase - Formylmethanofuran Dehydrogenase Complex From Methanospirillum Hungatei (Hexameric, Composite Structure) also contains other interesting chemical elements:

Iron (Fe) 212 atoms
Molybdenum (Mo) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Formate Dehydrogenase - Heterodisulfide Reductase - Formylmethanofuran Dehydrogenase Complex From Methanospirillum Hungatei (Hexameric, Composite Structure) (pdb code 7bkb). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Formate Dehydrogenase - Heterodisulfide Reductase - Formylmethanofuran Dehydrogenase Complex From Methanospirillum Hungatei (Hexameric, Composite Structure), PDB code: 7bkb:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 7bkb

Go back to Zinc Binding Sites List in 7bkb
Zinc binding site 1 out of 4 in the Formate Dehydrogenase - Heterodisulfide Reductase - Formylmethanofuran Dehydrogenase Complex From Methanospirillum Hungatei (Hexameric, Composite Structure)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Formate Dehydrogenase - Heterodisulfide Reductase - Formylmethanofuran Dehydrogenase Complex From Methanospirillum Hungatei (Hexameric, Composite Structure) within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Zn601

b:82.3
occ:1.00
 NE2 G:HIS60 2.0 51.0 1.0
OQ2 G:KCX184 2.0 50.8 1.0
OD1 G:ASP390 2.0 52.5 1.0
NE2 G:HIS58 2.0 51.8 1.0
CG G:ASP390 2.8 52.5 1.0
CX G:KCX184 2.9 50.8 1.0
CE1 G:HIS60 2.9 51.0 1.0
CD2 G:HIS60 2.9 51.0 1.0
CE1 G:HIS58 3.0 51.8 1.0
CD2 G:HIS58 3.0 51.8 1.0
OD2 G:ASP390 3.0 52.5 1.0
NZ G:KCX184 3.6 50.8 1.0
OQ1 G:KCX184 3.7 50.8 1.0
ND1 G:HIS60 3.9 51.0 1.0
CG G:HIS60 4.0 51.0 1.0
ND2 G:ASN393 4.0 49.3 1.0
ZN G:ZN602 4.0 96.7 1.0
ND1 G:HIS58 4.1 51.8 1.0
CG G:HIS58 4.1 51.8 1.0
CB G:ASP390 4.2 52.5 1.0
CD2 G:HIS276 4.4 52.2 1.0
CA G:ASP390 4.7 52.5 1.0
CE G:KCX184 4.7 50.8 1.0
CB G:ALA121 4.7 48.8 1.0
NE2 G:HIS276 4.7 52.2 1.0

Zinc binding site 2 out of 4 in 7bkb

Go back to Zinc Binding Sites List in 7bkb
Zinc binding site 2 out of 4 in the Formate Dehydrogenase - Heterodisulfide Reductase - Formylmethanofuran Dehydrogenase Complex From Methanospirillum Hungatei (Hexameric, Composite Structure)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Formate Dehydrogenase - Heterodisulfide Reductase - Formylmethanofuran Dehydrogenase Complex From Methanospirillum Hungatei (Hexameric, Composite Structure) within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Zn602

b:96.7
occ:1.00
 NE2 G:HIS237 1.8 54.7 1.0
NE2 G:HIS276 2.0 52.2 1.0
OQ1 G:KCX184 2.1 50.8 1.0
CE1 G:HIS237 2.4 54.7 1.0
CD2 G:HIS237 2.6 54.7 1.0
CX G:KCX184 2.8 50.8 1.0
OQ2 G:KCX184 2.8 50.8 1.0
CE1 G:HIS276 2.9 52.2 1.0
ND1 G:HIS237 3.0 54.7 1.0
CD2 G:HIS276 3.0 52.2 1.0
CG G:HIS237 3.2 54.7 1.0
OD2 G:ASP390 3.9 52.5 1.0
ND1 G:HIS276 4.0 52.2 1.0
NZ G:KCX184 4.0 50.8 1.0
ZN G:ZN601 4.0 82.3 1.0
CG G:HIS276 4.1 52.2 1.0
CG2 G:THR323 4.4 54.1 1.0
CB G:HIS237 4.4 54.7 1.0
CG2 G:THR275 4.6 50.4 1.0
CB G:THR323 4.7 54.1 1.0
CE G:KCX184 4.8 50.8 1.0
CA G:HIS237 4.8 54.7 1.0
CG G:ASP390 4.8 52.5 1.0
NE2 G:HIS58 4.9 51.8 1.0

Zinc binding site 3 out of 4 in 7bkb

Go back to Zinc Binding Sites List in 7bkb
Zinc binding site 3 out of 4 in the Formate Dehydrogenase - Heterodisulfide Reductase - Formylmethanofuran Dehydrogenase Complex From Methanospirillum Hungatei (Hexameric, Composite Structure)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Formate Dehydrogenase - Heterodisulfide Reductase - Formylmethanofuran Dehydrogenase Complex From Methanospirillum Hungatei (Hexameric, Composite Structure) within 5.0Å range:
probe atom residue distance (Å) B Occ
g:Zn601

b:82.3
occ:1.00
 NE2 g:HIS60 2.0 51.0 1.0
OQ1 g:KCX184 2.0 50.8 1.0
OD1 g:ASP390 2.0 52.5 1.0
NE2 g:HIS58 2.0 51.8 1.0
CG g:ASP390 2.8 52.5 1.0
CX g:KCX184 2.9 50.8 1.0
CE1 g:HIS60 2.9 51.0 1.0
CD2 g:HIS60 2.9 51.0 1.0
CE1 g:HIS58 3.0 51.8 1.0
CD2 g:HIS58 3.0 51.8 1.0
OD2 g:ASP390 3.0 52.5 1.0
NZ g:KCX184 3.6 50.8 1.0
OQ2 g:KCX184 3.7 50.8 1.0
ND1 g:HIS60 3.9 51.0 1.0
CG g:HIS60 4.0 51.0 1.0
ND2 g:ASN393 4.0 49.3 1.0
ZN g:ZN602 4.0 96.7 1.0
ND1 g:HIS58 4.1 51.8 1.0
CG g:HIS58 4.1 51.8 1.0
CB g:ASP390 4.2 52.5 1.0
CD2 g:HIS276 4.4 52.2 1.0
CA g:ASP390 4.7 52.5 1.0
CE g:KCX184 4.7 50.8 1.0
CB g:ALA121 4.7 48.8 1.0
NE2 g:HIS276 4.7 52.2 1.0

Zinc binding site 4 out of 4 in 7bkb

Go back to Zinc Binding Sites List in 7bkb
Zinc binding site 4 out of 4 in the Formate Dehydrogenase - Heterodisulfide Reductase - Formylmethanofuran Dehydrogenase Complex From Methanospirillum Hungatei (Hexameric, Composite Structure)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Formate Dehydrogenase - Heterodisulfide Reductase - Formylmethanofuran Dehydrogenase Complex From Methanospirillum Hungatei (Hexameric, Composite Structure) within 5.0Å range:
probe atom residue distance (Å) B Occ
g:Zn602

b:96.7
occ:1.00
 NE2 g:HIS237 1.8 54.7 1.0
NE2 g:HIS276 2.0 52.2 1.0
OQ2 g:KCX184 2.1 50.8 1.0
CE1 g:HIS237 2.4 54.7 1.0
CD2 g:HIS237 2.6 54.7 1.0
CX g:KCX184 2.8 50.8 1.0
OQ1 g:KCX184 2.8 50.8 1.0
CE1 g:HIS276 2.9 52.2 1.0
ND1 g:HIS237 3.0 54.7 1.0
CD2 g:HIS276 3.0 52.2 1.0
CG g:HIS237 3.2 54.7 1.0
OD2 g:ASP390 3.9 52.5 1.0
ND1 g:HIS276 4.0 52.2 1.0
NZ g:KCX184 4.0 50.8 1.0
ZN g:ZN601 4.0 82.3 1.0
CG g:HIS276 4.1 52.2 1.0
CG2 g:THR323 4.4 54.1 1.0
CB g:HIS237 4.4 54.7 1.0
CG2 g:THR275 4.6 50.4 1.0
CB g:THR323 4.7 54.1 1.0
CE g:KCX184 4.8 50.8 1.0
CA g:HIS237 4.8 54.7 1.0
CG g:ASP390 4.8 52.5 1.0
NE2 g:HIS58 4.9 51.8 1.0

Reference:

T.Watanabe, O.Pfeil-Gardiner, J.Kahnt, J.Koch, S.Shima, B.J.Murphy. Three-Megadalton Complex of Methanogenic Electron-Bifurcating and Co 2 -Fixing Enzymes. Science V. 373 1151 2021.
ISSN: ESSN 1095-9203
PubMed: 34516836
DOI: 10.1126/SCIENCE.ABG5550
Page generated: Tue Oct 29 17:37:39 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy