Iron in PDB 6zh5: Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor

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>>> Page 1 <<< Page 2, Binding sites: 11 - 16;

Binding sites:

The binding sites of Iron atom in the Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor (pdb code 6zh5). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 16 binding sites of Iron where determined in the Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor, PDB code: 6zh5:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 16 in the Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:138.2 occ:1.00 OE2 V:GLU131 2.2 102.8 1.0 OE2 G:GLU131 2.2 106.1 1.0 OE2 A:GLU131 2.2 106.0 1.0 CD V:GLU131 3.4 102.8 1.0 CD G:GLU131 3.4 106.1 1.0 CD A:GLU131 3.5 106.0 1.0 OE1 V:GLU131 4.0 102.8 1.0 OE1 G:GLU131 4.1 106.1 1.0 OE1 A:GLU131 4.1 106.0 1.0 CB A:GLU131 4.4 106.0 1.0 CB G:GLU131 4.5 106.1 1.0 CB V:GLU131 4.5 102.8 1.0 CG V:GLU131 4.5 102.8 1.0 CG A:GLU131 4.5 106.0 1.0 CG G:GLU131 4.6 106.1 1.0 FE A:FE202 4.7 115.7 1.0 CA A:ASP128 4.8 103.5 1.0 CA G:ASP128 4.8 107.9 1.0 OD1 A:ASP128 4.8 103.5 1.0 CA V:ASP128 4.8 103.0 1.0 OD1 G:ASP128 4.9 107.9 1.0 OD1 V:ASP128 5.0 103.0 1.0 CB G:ASP128 5.0 107.9 1.0 CB A:ASP128 5.0 103.5 1.0

Iron binding site 2 out of 16 in the Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe202 b:115.7 occ:1.00 OE1 A:GLU131 3.5 106.0 1.0 OE1 G:GLU131 3.6 106.1 1.0 OE1 V:GLU131 3.6 102.8 1.0 SG A:CYS127 3.9 104.1 1.0 SG G:CYS127 3.9 108.5 1.0 SG V:CYS127 4.0 103.9 1.0 CD A:GLU131 4.3 106.0 1.0 OE2 A:GLU131 4.3 106.0 1.0 CD G:GLU131 4.4 106.1 1.0 OE2 G:GLU131 4.5 106.1 1.0 CD V:GLU131 4.5 102.8 1.0 OE2 V:GLU131 4.5 102.8 1.0 FE A:FE201 4.7 138.2 1.0

Iron binding site 3 out of 16 in the Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:144.5 occ:1.00 OE2 F:GLU131 2.1 107.7 1.0 OE2 C:GLU131 2.2 109.7 1.0 OE2 N:GLU131 2.6 108.3 1.0 CD F:GLU131 3.3 107.7 1.0 CD C:GLU131 3.5 109.7 1.0 CD N:GLU131 3.8 108.3 1.0 OE1 F:GLU131 3.9 107.7 1.0 OE1 C:GLU131 4.1 109.7 1.0 CB F:GLU131 4.4 107.7 1.0 CG F:GLU131 4.4 107.7 1.0 CB C:GLU131 4.5 109.7 1.0 OE1 N:GLU131 4.5 108.3 1.0 CG C:GLU131 4.6 109.7 1.0 OD1 N:ASP128 4.6 109.6 1.0 CB N:GLU131 4.6 108.3 1.0 FE F:FE201 4.7 118.3 1.0 CA N:ASP128 4.8 109.6 1.0 CA F:ASP128 4.8 106.5 1.0 CA C:ASP128 4.8 108.1 1.0 CG N:GLU131 4.8 108.3 1.0 OD1 C:ASP128 4.9 108.1 1.0 CB N:ASP128 4.9 109.6 1.0 OD1 F:ASP128 4.9 106.5 1.0 CB C:ASP128 5.0 108.1 1.0

Iron binding site 4 out of 16 in the Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor within 5.0Å range: probe atom residue distance (Å) B Occ H:Fe201 b:143.0 occ:1.00 OE2 H:GLU131 2.0 110.9 1.0 OE2 R:GLU131 2.1 106.1 1.0 OE2 W:GLU131 2.2 108.5 1.0 CD H:GLU131 3.2 110.9 1.0 CD R:GLU131 3.2 106.1 1.0 CD W:GLU131 3.3 108.5 1.0 OE1 R:GLU131 3.7 106.1 1.0 OE1 H:GLU131 3.8 110.9 1.0 OE1 W:GLU131 3.9 108.5 1.0 CG H:GLU131 4.4 110.9 1.0 CB H:GLU131 4.4 110.9 1.0 CG R:GLU131 4.4 106.1 1.0 FE H:FE202 4.5 115.4 1.0 CB R:GLU131 4.5 106.1 1.0 CB W:GLU131 4.5 108.5 1.0 CG W:GLU131 4.5 108.5 1.0 CA H:ASP128 4.8 108.7 1.0 CA W:ASP128 4.8 110.6 1.0 CA R:ASP128 4.9 105.7 1.0 SG H:CYS127 5.0 109.4 1.0 SG R:CYS127 5.0 105.6 1.0

Iron binding site 5 out of 16 in the Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor within 5.0Å range: probe atom residue distance (Å) B Occ H:Fe202 b:115.4 occ:1.00 OE1 W:GLU131 3.5 108.5 1.0 OE1 H:GLU131 3.5 110.9 1.0 OE1 R:GLU131 3.7 106.1 1.0 SG W:CYS127 3.9 111.0 1.0 SG H:CYS127 4.0 109.4 1.0 SG R:CYS127 4.0 105.6 1.0 CD W:GLU131 4.4 108.5 1.0 OE2 W:GLU131 4.4 108.5 1.0 CD H:GLU131 4.4 110.9 1.0 OE2 H:GLU131 4.5 110.9 1.0 FE H:FE201 4.5 143.0 1.0 CD R:GLU131 4.6 106.1 1.0 OE2 R:GLU131 4.6 106.1 1.0

Iron binding site 6 out of 16 in the Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor within 5.0Å range: probe atom residue distance (Å) B Occ I:Fe201 b:114.2 occ:1.00 OE1 M:GLU131 3.5 104.3 1.0 OE1 I:GLU131 3.5 105.7 1.0 OE1 T:GLU131 3.6 103.0 1.0 SG T:CYS127 3.9 104.2 1.0 SG M:CYS127 3.9 106.0 1.0 SG I:CYS127 4.0 104.1 1.0 OE2 T:GLU131 4.3 103.0 1.0 OE2 M:GLU131 4.3 104.3 1.0 CD M:GLU131 4.3 104.3 1.0 CD T:GLU131 4.4 103.0 1.0 CD I:GLU131 4.4 105.7 1.0 OE2 I:GLU131 4.4 105.7 1.0 FE I:FE202 4.5 134.1 1.0

Iron binding site 7 out of 16 in the Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor within 5.0Å range: probe atom residue distance (Å) B Occ I:Fe202 b:134.1 occ:1.00 OE2 I:GLU131 2.0 105.7 1.0 OE2 M:GLU131 2.3 104.3 1.0 OE2 T:GLU131 2.5 103.0 1.0 CD I:GLU131 3.2 105.7 1.0 CD M:GLU131 3.5 104.3 1.0 CD T:GLU131 3.7 103.0 1.0 OE1 I:GLU131 3.8 105.7 1.0 OE1 M:GLU131 4.1 104.3 1.0 CG I:GLU131 4.4 105.7 1.0 OE1 T:GLU131 4.4 103.0 1.0 CB I:GLU131 4.4 105.7 1.0 FE I:FE201 4.5 114.2 1.0 CB M:GLU131 4.5 104.3 1.0 CG M:GLU131 4.6 104.3 1.0 CB T:GLU131 4.7 103.0 1.0 OD1 T:ASP128 4.7 103.4 1.0 CA I:ASP128 4.8 103.0 1.0 CA T:ASP128 4.8 103.4 1.0 CG T:GLU131 4.8 103.0 1.0 CA M:ASP128 4.8 105.5 1.0 CB T:ASP128 4.9 103.4 1.0 OD1 M:ASP128 4.9 105.5 1.0 SG I:CYS127 5.0 104.1 1.0

Iron binding site 8 out of 16 in the Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor within 5.0Å range: probe atom residue distance (Å) B Occ J:Fe201 b:144.0 occ:1.00 OE2 Q:GLU131 2.1 106.2 1.0 OE2 J:GLU131 2.1 105.2 1.0 OE2 P:GLU131 2.2 105.5 1.0 CD Q:GLU131 3.2 106.2 1.0 CD J:GLU131 3.3 105.2 1.0 CD P:GLU131 3.4 105.5 1.0 OE1 Q:GLU131 3.8 106.2 1.0 OE1 J:GLU131 3.9 105.2 1.0 OE1 P:GLU131 4.0 105.5 1.0 CG Q:GLU131 4.4 106.2 1.0 CG J:GLU131 4.5 105.2 1.0 CB Q:GLU131 4.5 106.2 1.0 CB J:GLU131 4.5 105.2 1.0 FE J:FE202 4.5 114.2 1.0 CB P:GLU131 4.6 105.5 1.0 CG P:GLU131 4.6 105.5 1.0 CA J:ASP128 4.8 105.6 1.0 CA Q:ASP128 4.8 105.1 1.0 CA P:ASP128 4.9 105.7 1.0 SG Q:CYS127 5.0 106.0 1.0

Iron binding site 9 out of 16 in the Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor within 5.0Å range: probe atom residue distance (Å) B Occ J:Fe202 b:114.2 occ:1.00 OE1 P:GLU131 3.5 105.5 1.0 OE1 J:GLU131 3.6 105.2 1.0 OE1 Q:GLU131 3.6 106.2 1.0 SG J:CYS127 3.9 105.8 1.0 SG Q:CYS127 4.0 106.0 1.0 SG P:CYS127 4.1 106.1 1.0 CD P:GLU131 4.4 105.5 1.0 OE2 P:GLU131 4.4 105.5 1.0 CD J:GLU131 4.4 105.2 1.0 OE2 J:GLU131 4.5 105.2 1.0 FE J:FE201 4.5 144.0 1.0 CD Q:GLU131 4.5 106.2 1.0 OE2 Q:GLU131 4.6 106.2 1.0

Iron binding site 10 out of 16 in the Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Folding of An Iron Binding Peptide in Response to Sedimentation Is Resolved Using Ferritin As A Nano-Reactor within 5.0Å range: probe atom residue distance (Å) B Occ K:Fe201 b:136.7 occ:1.00 OE2 U:GLU131 2.0 110.5 1.0 OE2 K:GLU131 2.2 105.3 1.0 OE2 S:GLU131 2.5 105.3 1.0 CD U:GLU131 3.2 110.5 1.0 CD K:GLU131 3.4 105.3 1.0 CD S:GLU131 3.7 105.3 1.0 OE1 U:GLU131 3.8 110.5 1.0 OE1 K:GLU131 4.0 105.3 1.0 OE1 S:GLU131 4.4 105.3 1.0 CG U:GLU131 4.4 110.5 1.0 CB U:GLU131 4.4 110.5 1.0 FE U:FE201 4.5 117.0 1.0 CG K:GLU131 4.6 105.3 1.0 CB K:GLU131 4.6 105.3 1.0 CB S:GLU131 4.7 105.3 1.0 CA U:ASP128 4.7 108.9 1.0 OD1 S:ASP128 4.7 103.8 1.0 CA S:ASP128 4.8 103.8 1.0 CG S:GLU131 4.8 105.3 1.0 CA K:ASP128 4.9 107.6 1.0 CB S:ASP128 4.9 103.8 1.0 CB U:ASP128 4.9 108.9 1.0 SG U:CYS127 4.9 109.8 1.0 OD1 U:ASP128 5.0 108.9 1.0

G.Davidov, G.Abelya, R.Zalk, B.Izbicki, S.Shaibi, L.Spektor, D.Shagidov, E.G.Meyron-Holtz, R.Zarivach, G.A.Frank. Folding of An Intrinsically Disordered Iron-Binding Peptide in Response to Sedimentation Revealed By Cryo-Em. J.Am.Chem.Soc. V. 142 19551 2020.
ISSN: ESSN 1520-5126
PubMed: 33166133
DOI: 10.1021/JACS.0C07565