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Iron in PDB 2auv: Solution Structure of Hndac : A Thioredoxin-Like [2FE-2S] Ferredoxin Involved in the Nadp-Reducing Hydrogenase Complex

Enzymatic activity of Solution Structure of Hndac : A Thioredoxin-Like [2FE-2S] Ferredoxin Involved in the Nadp-Reducing Hydrogenase Complex

All present enzymatic activity of Solution Structure of Hndac : A Thioredoxin-Like [2FE-2S] Ferredoxin Involved in the Nadp-Reducing Hydrogenase Complex:
1.12.1.3;

Iron Binding Sites:

The binding sites of Iron atom in the Solution Structure of Hndac : A Thioredoxin-Like [2FE-2S] Ferredoxin Involved in the Nadp-Reducing Hydrogenase Complex (pdb code 2auv). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Solution Structure of Hndac : A Thioredoxin-Like [2FE-2S] Ferredoxin Involved in the Nadp-Reducing Hydrogenase Complex, PDB code: 2auv:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 2auv

Go back to Iron Binding Sites List in 2auv
Iron binding site 1 out of 2 in the Solution Structure of Hndac : A Thioredoxin-Like [2FE-2S] Ferredoxin Involved in the Nadp-Reducing Hydrogenase Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Solution Structure of Hndac : A Thioredoxin-Like [2FE-2S] Ferredoxin Involved in the Nadp-Reducing Hydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe86

b:2.4
occ:1.00
FE1 A:FES86 0.0 2.4 1.0
S1 A:FES86 2.2 3.0 1.0
SG A:CYS17 2.2 2.8 1.0
S2 A:FES86 2.4 2.9 1.0
SG A:CYS12 2.8 2.2 1.0
HB2 A:CYS12 3.1 1.9 1.0
HB1 A:ALA58 3.2 3.9 1.0
CB A:CYS12 3.3 1.8 1.0
HA A:VAL54 3.4 3.6 1.0
CB A:CYS17 3.4 2.3 1.0
HB3 A:CYS12 3.4 1.8 1.0
HB2 A:CYS17 3.4 2.3 1.0
HB3 A:CYS17 3.7 2.1 1.0
FE2 A:FES86 3.8 2.9 1.0
HG13 A:VAL54 4.1 4.6 1.0
HG21 A:VAL54 4.2 4.0 1.0
CB A:ALA58 4.3 3.6 1.0
H A:VAL54 4.4 3.0 1.0
CA A:VAL54 4.4 3.3 1.0
H A:CYS17 4.5 3.1 1.0
H A:ALA58 4.5 3.3 1.0
HB2 A:ALA58 4.5 3.9 1.0
CA A:CYS17 4.7 2.5 1.0
HA A:ALA58 4.8 2.9 1.0
CA A:CYS12 4.8 1.6 1.0
N A:VAL54 4.8 2.9 1.0
HB3 A:ALA58 4.9 3.9 1.0
H A:CYS57 4.9 3.5 1.0
HB2 A:CYS57 5.0 2.8 1.0
N A:CYS17 5.0 3.0 1.0
CG1 A:VAL54 5.0 4.3 1.0

Iron binding site 2 out of 2 in 2auv

Go back to Iron Binding Sites List in 2auv
Iron binding site 2 out of 2 in the Solution Structure of Hndac : A Thioredoxin-Like [2FE-2S] Ferredoxin Involved in the Nadp-Reducing Hydrogenase Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Solution Structure of Hndac : A Thioredoxin-Like [2FE-2S] Ferredoxin Involved in the Nadp-Reducing Hydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe86

b:2.9
occ:1.00
FE2 A:FES86 0.0 2.9 1.0
H A:VAL54 1.9 3.0 1.0
S2 A:FES86 2.2 2.9 1.0
SG A:CYS57 2.2 3.3 1.0
H A:GLY55 2.3 3.0 1.0
N A:VAL54 2.6 2.9 1.0
HA A:VAL54 2.7 3.6 1.0
N A:GLY55 3.0 3.3 1.0
HB2 A:CYS57 3.0 2.8 1.0
CA A:VAL54 3.1 3.3 1.0
SG A:CYS53 3.1 3.0 1.0
CB A:CYS57 3.2 3.0 1.0
HB2 A:CYS12 3.5 1.9 1.0
C A:VAL54 3.5 3.5 1.0
S1 A:FES86 3.5 3.0 1.0
HA A:CYS53 3.6 2.7 1.0
H A:CYS57 3.7 3.5 1.0
C A:CYS53 3.7 2.6 1.0
FE1 A:FES86 3.8 2.4 1.0
HB3 A:CYS57 4.0 3.1 1.0
CA A:CYS53 4.1 2.5 1.0
H A:GLY56 4.1 4.1 1.0
CA A:GLY55 4.1 3.8 1.0
N A:CYS57 4.1 3.5 1.0
C A:GLY55 4.1 4.0 1.0
N A:GLY56 4.2 4.1 1.0
CB A:CYS53 4.2 2.6 1.0
CA A:CYS57 4.3 3.2 1.0
H A:ALA58 4.3 3.3 1.0
CB A:CYS12 4.5 1.8 1.0
CB A:VAL54 4.5 3.7 1.0
HA3 A:GLY55 4.6 3.9 1.0
O A:VAL54 4.6 4.0 1.0
HB A:ILE62 4.6 2.1 1.0
HG22 A:ILE62 4.7 2.8 1.0
O A:GLY55 4.7 4.2 1.0
N A:ALA58 4.7 3.1 1.0
HG21 A:VAL54 4.8 4.0 1.0
O A:CYS53 4.8 2.8 1.0
HG23 A:VAL54 4.8 3.9 1.0
HB3 A:CYS53 4.9 2.6 1.0
HB3 A:CYS12 4.9 1.8 1.0
HA2 A:GLY55 4.9 4.2 1.0
C A:GLY56 4.9 4.0 1.0
HB2 A:CYS53 4.9 2.7 1.0
C A:CYS57 5.0 3.1 1.0
HB1 A:ALA58 5.0 3.9 1.0
CG2 A:VAL54 5.0 3.8 1.0

Reference:

M.Nouailler, X.Morelli, O.Bornet, B.Chetrit, Z.Dermoun, F.Guerlesquin. Solution Structure of Hndac: A Thioredoxin-Like Domain Involved in the Nadp-Reducing Hydrogenase Complex Protein Sci. V. 15 1369 2006.
ISSN: ISSN 0961-8368
PubMed: 16731971
DOI: 10.1110/PS.051916606
Page generated: Sun Dec 13 14:40:07 2020

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