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Iron in PDB 1dox: 1H and 15N Sequential Assignment, Secondary Structure and Tertiary Fold of [2FE-2S] Ferredoxin From Synechocystis Sp. Pcc 6803

Iron Binding Sites:

The binding sites of Iron atom in the 1H and 15N Sequential Assignment, Secondary Structure and Tertiary Fold of [2FE-2S] Ferredoxin From Synechocystis Sp. Pcc 6803 (pdb code 1dox). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the 1H and 15N Sequential Assignment, Secondary Structure and Tertiary Fold of [2FE-2S] Ferredoxin From Synechocystis Sp. Pcc 6803, PDB code: 1dox:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1dox

Go back to Iron Binding Sites List in 1dox
Iron binding site 1 out of 2 in the 1H and 15N Sequential Assignment, Secondary Structure and Tertiary Fold of [2FE-2S] Ferredoxin From Synechocystis Sp. Pcc 6803


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 1H and 15N Sequential Assignment, Secondary Structure and Tertiary Fold of [2FE-2S] Ferredoxin From Synechocystis Sp. Pcc 6803 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe97

b:0.0
occ:1.00
FE1 A:FES97 0.0 0.0 1.0
SG A:CYS44 2.3 0.0 1.0
SG A:CYS39 2.3 0.0 1.0
H A:CYS44 2.4 0.0 1.0
FE2 A:FES97 2.8 0.0 1.0
H A:ALA43 2.8 0.0 1.0
H A:ARG40 3.0 0.0 1.0
N A:CYS44 3.3 0.0 1.0
H A:CYS39 3.4 0.0 1.0
CB A:CYS44 3.6 0.0 1.0
CB A:CYS39 3.6 0.0 1.0
HB3 A:CYS39 3.6 0.0 1.0
CA A:CYS44 3.8 0.0 1.0
N A:ALA43 3.8 0.0 1.0
N A:ARG40 3.8 0.0 1.0
HA2 A:GLY42 3.8 0.0 1.0
O A:CYS44 3.8 0.0 1.0
C A:CYS44 3.9 0.0 1.0
HB3 A:CYS44 4.0 0.0 1.0
H A:THR46 4.0 0.0 1.0
N A:CYS39 4.1 0.0 1.0
CA A:CYS39 4.3 0.0 1.0
HB3 A:PRO36 4.3 0.0 1.0
HB2 A:SER38 4.3 0.0 1.0
SG A:CYS77 4.3 0.0 1.0
H A:ALA41 4.4 0.0 1.0
C A:ALA43 4.4 0.0 1.0
HB2 A:PRO36 4.4 0.0 1.0
N A:GLY42 4.4 0.0 1.0
CA A:GLY42 4.4 0.0 1.0
OG1 A:THR46 4.5 0.0 1.0
HB2 A:CYS39 4.5 0.0 1.0
C A:CYS39 4.5 0.0 1.0
HB2 A:CYS44 4.5 0.0 1.0
SG A:CYS47 4.5 0.0 1.0
H A:GLY42 4.5 0.0 1.0
HG1 A:THR46 4.6 0.0 1.0
C A:GLY42 4.6 0.0 1.0
HA A:ARG40 4.6 0.0 1.0
N A:SER45 4.6 0.0 1.0
N A:ALA41 4.6 0.0 1.0
CA A:ALA43 4.6 0.0 1.0
CA A:ARG40 4.7 0.0 1.0
HB1 A:ALA43 4.8 0.0 1.0
C A:ALA41 4.8 0.0 1.0
HA A:CYS44 4.8 0.0 1.0
C A:ARG40 4.8 0.0 1.0
CB A:PRO36 4.9 0.0 1.0
H A:CYS47 5.0 0.0 1.0
N A:THR46 5.0 0.0 1.0

Iron binding site 2 out of 2 in 1dox

Go back to Iron Binding Sites List in 1dox
Iron binding site 2 out of 2 in the 1H and 15N Sequential Assignment, Secondary Structure and Tertiary Fold of [2FE-2S] Ferredoxin From Synechocystis Sp. Pcc 6803


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of 1H and 15N Sequential Assignment, Secondary Structure and Tertiary Fold of [2FE-2S] Ferredoxin From Synechocystis Sp. Pcc 6803 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe97

b:0.0
occ:1.00
FE2 A:FES97 0.0 0.0 1.0
SG A:CYS77 2.3 0.0 1.0
SG A:CYS47 2.3 0.0 1.0
FE1 A:FES97 2.8 0.0 1.0
H A:CYS77 3.4 0.0 1.0
HB3 A:CYS77 3.5 0.0 1.0
HB3 A:CYS47 3.5 0.0 1.0
CB A:CYS77 3.6 0.0 1.0
HA2 A:GLY42 3.6 0.0 1.0
CB A:CYS47 3.6 0.0 1.0
H A:CYS47 4.1 0.0 1.0
HB2 A:CYS47 4.2 0.0 1.0
N A:CYS77 4.2 0.0 1.0
H A:ALA43 4.2 0.0 1.0
HB2 A:CYS77 4.3 0.0 1.0
HA A:LEU75 4.3 0.0 1.0
O A:CYS44 4.3 0.0 1.0
SG A:CYS39 4.4 0.0 1.0
HD11 A:LEU75 4.4 0.0 1.0
H A:CYS44 4.4 0.0 1.0
O A:ALA41 4.4 0.0 1.0
SG A:CYS44 4.5 0.0 1.0
H A:THR76 4.5 0.0 1.0
CA A:CYS77 4.5 0.0 1.0
CA A:GLY42 4.6 0.0 1.0
N A:CYS47 4.6 0.0 1.0
O A:VAL74 4.7 0.0 1.0
H A:THR46 4.7 0.0 1.0
HB3 A:PRO36 4.7 0.0 1.0
CA A:CYS47 4.8 0.0 1.0
OG1 A:THR76 4.8 0.0 1.0
HA A:SER45 4.8 0.0 1.0
C A:ALA41 4.8 0.0 1.0
HB2 A:PRO36 4.9 0.0 1.0
H A:ARG40 4.9 0.0 1.0
N A:GLY42 4.9 0.0 1.0
HG22 A:THR76 4.9 0.0 1.0
N A:THR76 4.9 0.0 1.0
C A:CYS44 5.0 0.0 1.0

Reference:

C.Lelong, P.Setif, H.Bottin, F.Andre, J.M.Neumann. 1H and 15N uc(Nmr) Sequential Assignment, Secondary Structure, and Tertiary Fold of [2FE-2S] Ferredoxin From Synechocystis Sp. Pcc 6803. Biochemistry V. 34 14462 1995.
ISSN: ISSN 0006-2960
PubMed: 7578051
DOI: 10.1021/BI00044A024
Page generated: Wed Jul 16 13:23:18 2025

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