Atomistry » Iron » PDB 6tmf-6u8y » 6tqm
Atomistry »
  Iron »
    PDB 6tmf-6u8y »
      6tqm »

Iron in PDB 6tqm: Escherichia Coli Adhe Structure in Its Compact Conformation

Enzymatic activity of Escherichia Coli Adhe Structure in Its Compact Conformation

All present enzymatic activity of Escherichia Coli Adhe Structure in Its Compact Conformation:
1.1.1.1; 1.2.1.10;

Iron Binding Sites:

The binding sites of Iron atom in the Escherichia Coli Adhe Structure in Its Compact Conformation (pdb code 6tqm). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Escherichia Coli Adhe Structure in Its Compact Conformation, PDB code: 6tqm:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 6tqm

Go back to Iron Binding Sites List in 6tqm
Iron binding site 1 out of 2 in the Escherichia Coli Adhe Structure in Its Compact Conformation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Escherichia Coli Adhe Structure in Its Compact Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe901

b:0.6
occ:1.00
HE1 B:HIS737 1.7 0.2 1.0
NE2 B:HIS657 2.1 0.6 1.0
OD2 B:ASP653 2.1 0.6 1.0
NE2 B:HIS723 2.1 0.6 1.0
CE1 B:HIS737 2.1 0.2 1.0
OD1 B:ASP653 2.2 0.6 1.0
NE2 B:HIS737 2.3 0.2 1.0
CG B:ASP653 2.4 0.6 1.0
CD2 B:HIS657 2.9 0.6 1.0
CD2 B:HIS723 3.0 0.6 1.0
CE1 B:HIS657 3.1 0.6 1.0
HD2 B:HIS657 3.1 0.6 1.0
HD2 B:HIS723 3.1 0.6 1.0
HD21 B:ASN741 3.1 0.8 1.0
CE1 B:HIS723 3.2 0.6 1.0
HE1 B:HIS657 3.3 0.6 1.0
ND1 B:HIS737 3.3 0.2 1.0
HE1 B:HIS723 3.4 0.6 1.0
CD2 B:HIS737 3.6 0.2 1.0
HD22 B:ASN741 3.7 0.8 1.0
ND2 B:ASN741 3.8 0.8 1.0
HD1 B:HIS737 3.8 0.2 1.0
CB B:ASP653 3.9 0.6 1.0
H5N B:TXE902 3.9 0.9 1.0
CG B:HIS657 4.0 0.6 1.0
ND1 B:HIS657 4.1 0.6 1.0
CG B:HIS737 4.1 0.2 1.0
HB3 B:ASP653 4.2 0.6 1.0
CG B:HIS723 4.2 0.6 1.0
ND1 B:HIS723 4.2 0.6 1.0
HD2 B:HIS737 4.3 0.2 1.0
HB2 B:ASP653 4.4 0.6 1.0
HA B:ASP653 4.5 0.6 1.0
HG1 B:THR601 4.7 0.3 1.0
CA B:ASP653 4.7 0.6 1.0
O B:ASP653 4.8 0.6 1.0
C5N B:TXE902 4.8 0.9 1.0
HD1 B:HIS657 4.8 0.6 1.0
CG B:ASN741 5.0 0.8 1.0

Iron binding site 2 out of 2 in 6tqm

Go back to Iron Binding Sites List in 6tqm
Iron binding site 2 out of 2 in the Escherichia Coli Adhe Structure in Its Compact Conformation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Escherichia Coli Adhe Structure in Its Compact Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe901

b:0.2
occ:1.00
HE1 A:HIS737 1.7 0.4 1.0
NE2 A:HIS657 2.1 0.5 1.0
OD2 A:ASP653 2.1 0.8 1.0
NE2 A:HIS723 2.1 0.4 1.0
CE1 A:HIS737 2.1 0.4 1.0
OD1 A:ASP653 2.2 0.8 1.0
NE2 A:HIS737 2.3 0.4 1.0
CG A:ASP653 2.4 0.8 1.0
CD2 A:HIS657 2.9 0.5 1.0
CD2 A:HIS723 3.0 0.4 1.0
CE1 A:HIS657 3.1 0.5 1.0
HD2 A:HIS657 3.1 0.5 1.0
HD2 A:HIS723 3.1 0.4 1.0
HD21 A:ASN741 3.1 0.5 1.0
CE1 A:HIS723 3.2 0.4 1.0
HE1 A:HIS657 3.3 0.5 1.0
ND1 A:HIS737 3.3 0.4 1.0
HE1 A:HIS723 3.4 0.4 1.0
CD2 A:HIS737 3.6 0.4 1.0
HD22 A:ASN741 3.7 0.5 1.0
ND2 A:ASN741 3.8 0.5 1.0
HD1 A:HIS737 3.8 0.4 1.0
H5N A:TXE902 3.9 0.3 1.0
CB A:ASP653 3.9 0.8 1.0
CG A:HIS657 4.0 0.5 1.0
ND1 A:HIS657 4.1 0.5 1.0
CG A:HIS737 4.1 0.4 1.0
HB3 A:ASP653 4.2 0.8 1.0
CG A:HIS723 4.2 0.4 1.0
ND1 A:HIS723 4.2 0.4 1.0
HD2 A:HIS737 4.3 0.4 1.0
HB2 A:ASP653 4.4 0.8 1.0
HA A:ASP653 4.5 0.8 1.0
HG1 A:THR601 4.7 0.2 1.0
CA A:ASP653 4.7 0.8 1.0
O A:ASP653 4.8 0.8 1.0
C5N A:TXE902 4.8 0.3 1.0
HD1 A:HIS657 4.8 0.5 1.0
CG A:ASN741 5.0 0.5 1.0

Reference:

P.Pony, C.Rapisarda, L.Terradot, E.Marza, R.Fronzes. Filamentation of the Bacterial Bi-Functional Alcohol/Aldehyde Dehydrogenase Adhe Is Essential For Substrate Channeling and Enzymatic Regulation. Nat Commun V. 11 1426 2020.
ISSN: ESSN 2041-1723
PubMed: 32188856
DOI: 10.1038/S41467-020-15214-Y
Page generated: Wed Aug 7 11:30:06 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy