Atomistry » Iron » PDB 2g6o-2grx » 2gmh
Atomistry »
  Iron »
    PDB 2g6o-2grx »
      2gmh »

Iron in PDB 2gmh: Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone

Enzymatic activity of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone

All present enzymatic activity of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone:
1.5.5.1;

Protein crystallography data

The structure of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone, PDB code: 2gmh was solved by J.Zhang, F.E.Frerman, J.-J.P.Kim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.67 / 2.50
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 154.322, 154.322, 128.536, 90.00, 90.00, 90.00
R / Rfree (%) 22.1 / 25.4

Other elements in 2gmh:

The structure of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone also contains other interesting chemical elements:

Sodium (Na) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone (pdb code 2gmh). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone, PDB code: 2gmh:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in 2gmh

Go back to Iron Binding Sites List in 2gmh
Iron binding site 1 out of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe610

b:19.3
occ:1.00
 FE1 A:SF4610 0.0 19.3 1.0
S2 A:SF4610 2.3 19.4 1.0
S4 A:SF4610 2.3 19.3 1.0
S3 A:SF4610 2.3 16.7 1.0
SG A:CYS553 2.3 23.1 1.0
FE4 A:SF4610 2.7 22.5 1.0
FE2 A:SF4610 2.7 18.0 1.0
FE3 A:SF4610 2.8 22.7 1.0
CB A:CYS553 3.4 26.8 1.0
CA A:CYS553 3.7 26.1 1.0
S1 A:SF4610 3.9 18.0 1.0
N A:VAL554 3.9 23.1 1.0
N A:HIS555 4.0 19.4 1.0
CD1 A:LEU504 4.2 29.6 1.0
C A:CYS553 4.2 26.5 1.0
NE1 A:TRP570 4.4 22.5 1.0
CG2 A:VAL532 4.4 25.6 1.0
CA A:HIS555 4.5 21.6 1.0
N A:CYS556 4.6 19.7 1.0
CD1 A:TRP570 4.7 21.2 1.0
SG A:CYS528 4.8 20.5 1.0
SG A:CYS556 4.8 22.3 1.0
SG A:CYS559 4.9 20.5 1.0
CG A:LEU504 4.9 32.3 1.0
C A:VAL554 4.9 20.1 1.0
N A:CYS553 4.9 24.6 1.0
CD2 A:LEU504 4.9 30.0 1.0
CA A:VAL554 5.0 21.0 1.0

Iron binding site 2 out of 8 in 2gmh

Go back to Iron Binding Sites List in 2gmh
Iron binding site 2 out of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe610

b:18.0
occ:1.00
 FE2 A:SF4610 0.0 18.0 1.0
SG A:CYS528 2.2 20.5 1.0
S1 A:SF4610 2.3 18.0 1.0
S4 A:SF4610 2.3 19.3 1.0
S3 A:SF4610 2.3 16.7 1.0
FE4 A:SF4610 2.7 22.5 1.0
FE1 A:SF4610 2.7 19.3 1.0
FE3 A:SF4610 2.8 22.7 1.0
CB A:CYS528 3.4 23.7 1.0
S2 A:SF4610 3.8 19.4 1.0
CD A:PRO529 3.9 24.2 1.0
CA A:CYS528 4.0 25.8 1.0
CG2 A:VAL532 4.0 25.6 1.0
CB A:VAL532 4.2 23.4 1.0
N A:PRO529 4.5 26.0 1.0
C A:CYS528 4.5 25.4 1.0
CB A:ALA530 4.6 16.8 1.0
CE1 A:TYR533 4.6 17.8 1.0
N A:ALA530 4.6 22.3 1.0
SG A:CYS556 4.7 22.3 1.0
CG A:PRO529 4.7 21.8 1.0
SG A:CYS559 4.7 20.5 1.0
SG A:CYS553 5.0 23.1 1.0

Iron binding site 3 out of 8 in 2gmh

Go back to Iron Binding Sites List in 2gmh
Iron binding site 3 out of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe610

b:22.7
occ:1.00
 FE3 A:SF4610 0.0 22.7 1.0
S4 A:SF4610 2.2 19.3 1.0
SG A:CYS556 2.2 22.3 1.0
S2 A:SF4610 2.3 19.4 1.0
S1 A:SF4610 2.3 18.0 1.0
FE4 A:SF4610 2.7 22.5 1.0
FE2 A:SF4610 2.8 18.0 1.0
FE1 A:SF4610 2.8 19.3 1.0
N A:CYS556 3.6 19.7 1.0
CB A:CYS556 3.6 20.7 1.0
N A:LYS557 3.8 18.6 1.0
S3 A:SF4610 3.9 16.7 1.0
CD A:PRO529 3.9 24.2 1.0
CA A:CYS556 4.0 21.6 1.0
N A:THR558 4.0 20.4 1.0
CG A:PRO529 4.2 21.8 1.0
C A:CYS556 4.4 20.5 1.0
CB A:THR558 4.5 17.4 1.0
C A:HIS555 4.6 20.8 1.0
CA A:LYS557 4.7 17.8 1.0
SG A:CYS528 4.7 20.5 1.0
CG2 A:VAL554 4.7 19.1 1.0
N A:HIS555 4.7 19.4 1.0
SG A:CYS559 4.7 20.5 1.0
N A:CYS559 4.7 21.6 1.0
OG1 A:THR558 4.8 21.5 1.0
SG A:CYS553 4.8 23.1 1.0
C A:LYS557 4.8 20.7 1.0
CA A:THR558 4.8 19.9 1.0
CA A:HIS555 4.9 21.6 1.0

Iron binding site 4 out of 8 in 2gmh

Go back to Iron Binding Sites List in 2gmh
Iron binding site 4 out of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe610

b:22.5
occ:1.00
 FE4 A:SF4610 0.0 22.5 1.0
S2 A:SF4610 2.2 19.4 1.0
S1 A:SF4610 2.2 18.0 1.0
S3 A:SF4610 2.2 16.7 1.0
SG A:CYS559 2.3 20.5 1.0
FE3 A:SF4610 2.7 22.7 1.0
FE1 A:SF4610 2.7 19.3 1.0
FE2 A:SF4610 2.7 18.0 1.0
CB A:CYS559 3.3 19.6 1.0
S4 A:SF4610 3.8 19.3 1.0
N A:CYS559 3.8 21.6 1.0
CD1 A:LEU504 3.9 29.6 1.0
CA A:CYS559 4.2 21.7 1.0
OH A:TYR533 4.3 21.3 1.0
CE1 A:TYR533 4.4 17.8 1.0
CD1 A:TRP570 4.6 21.2 1.0
SG A:CYS556 4.6 22.3 1.0
N A:THR558 4.6 20.4 1.0
SG A:CYS553 4.7 23.1 1.0
SG A:CYS528 4.7 20.5 1.0
CG A:LEU504 4.8 32.3 1.0
CZ A:TYR533 4.8 22.5 1.0
C A:THR558 5.0 21.3 1.0
N A:LYS557 5.0 18.6 1.0

Iron binding site 5 out of 8 in 2gmh

Go back to Iron Binding Sites List in 2gmh
Iron binding site 5 out of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe613

b:59.8
occ:1.00
 FE1 B:SF4613 0.0 59.8 1.0
S2 B:SF4613 2.3 57.4 1.0
S4 B:SF4613 2.3 58.4 1.0
S3 B:SF4613 2.3 59.0 1.0
SG B:CYS553 2.5 69.5 1.0
FE4 B:SF4613 2.7 59.3 1.0
FE3 B:SF4613 2.8 59.8 1.0
FE2 B:SF4613 2.8 59.2 1.0
CB B:CYS553 3.1 67.7 1.0
CA B:CYS553 3.3 67.6 1.0
N B:VAL554 3.7 66.4 1.0
S1 B:SF4613 3.9 56.0 1.0
C B:CYS553 3.9 67.2 1.0
N B:HIS555 4.1 64.4 1.0
CG2 B:VAL532 4.4 67.4 1.0
N B:CYS553 4.5 67.6 1.0
N B:CYS556 4.6 61.9 1.0
NE1 B:TRP570 4.7 53.5 1.0
CA B:HIS555 4.7 63.9 1.0
CD1 B:LEU504 4.8 66.5 1.0
CD1 B:TRP570 4.8 54.4 1.0
SG B:CYS528 4.8 53.4 1.0
SG B:CYS556 4.9 66.8 1.0
CA B:VAL554 4.9 65.8 1.0
SG B:CYS559 4.9 52.2 1.0
C B:VAL554 4.9 65.3 1.0
O B:CYS553 4.9 67.6 1.0

Iron binding site 6 out of 8 in 2gmh

Go back to Iron Binding Sites List in 2gmh
Iron binding site 6 out of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe613

b:59.2
occ:1.00
 FE2 B:SF4613 0.0 59.2 1.0
SG B:CYS528 2.3 53.4 1.0
S1 B:SF4613 2.3 56.0 1.0
S3 B:SF4613 2.3 59.0 1.0
S4 B:SF4613 2.3 58.4 1.0
FE4 B:SF4613 2.7 59.3 1.0
FE1 B:SF4613 2.8 59.8 1.0
FE3 B:SF4613 2.8 59.8 1.0
CB B:CYS528 3.6 57.3 1.0
CD B:PRO529 3.7 59.0 1.0
S2 B:SF4613 3.9 57.4 1.0
CG2 B:VAL532 4.0 67.4 1.0
CA B:CYS528 4.1 57.6 1.0
CE1 B:TYR533 4.3 69.8 1.0
CB B:VAL532 4.4 68.3 1.0
CG B:PRO529 4.5 59.5 1.0
N B:PRO529 4.5 58.9 1.0
CB B:ALA530 4.6 63.7 1.0
N B:ALA530 4.6 63.9 1.0
C B:CYS528 4.6 58.1 1.0
SG B:CYS559 4.7 52.2 1.0
SG B:CYS556 4.7 66.8 1.0
CA B:CYS553 4.9 67.6 1.0
CD1 B:TYR533 4.9 69.8 1.0

Iron binding site 7 out of 8 in 2gmh

Go back to Iron Binding Sites List in 2gmh
Iron binding site 7 out of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe613

b:59.8
occ:1.00
 FE3 B:SF4613 0.0 59.8 1.0
S4 B:SF4613 2.2 58.4 1.0
SG B:CYS556 2.3 66.8 1.0
S2 B:SF4613 2.3 57.4 1.0
S1 B:SF4613 2.3 56.0 1.0
FE4 B:SF4613 2.7 59.3 1.0
FE1 B:SF4613 2.8 59.8 1.0
FE2 B:SF4613 2.8 59.2 1.0
CB B:CYS556 3.6 61.7 1.0
N B:CYS556 3.7 61.9 1.0
S3 B:SF4613 3.9 59.0 1.0
CD B:PRO529 3.9 59.0 1.0
CG B:PRO529 3.9 59.5 1.0
N B:LYS557 3.9 60.0 1.0
CA B:CYS556 4.0 61.5 1.0
N B:THR558 4.2 56.6 1.0
C B:CYS556 4.3 60.2 1.0
CB B:THR558 4.4 54.4 1.0
OG1 B:THR558 4.6 54.3 1.0
SG B:CYS559 4.7 52.2 1.0
SG B:CYS528 4.7 53.4 1.0
N B:CYS559 4.8 55.9 1.0
C B:HIS555 4.8 62.6 1.0
CG2 B:VAL554 4.8 66.5 1.0
N B:HIS555 4.8 64.4 1.0
CA B:THR558 4.9 55.8 1.0
CA B:LYS557 4.9 58.7 1.0
N B:VAL554 4.9 66.4 1.0
SG B:CYS553 4.9 69.5 1.0
C B:LYS557 5.0 57.5 1.0

Iron binding site 8 out of 8 in 2gmh

Go back to Iron Binding Sites List in 2gmh
Iron binding site 8 out of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe613

b:59.3
occ:1.00
 FE4 B:SF4613 0.0 59.3 1.0
S1 B:SF4613 2.2 56.0 1.0
S2 B:SF4613 2.2 57.4 1.0
S3 B:SF4613 2.2 59.0 1.0
SG B:CYS559 2.3 52.2 1.0
FE3 B:SF4613 2.7 59.8 1.0
FE1 B:SF4613 2.7 59.8 1.0
FE2 B:SF4613 2.7 59.2 1.0
CB B:CYS559 3.4 54.2 1.0
S4 B:SF4613 3.8 58.4 1.0
N B:CYS559 3.9 55.9 1.0
OH B:TYR533 4.1 68.8 1.0
CD1 B:LEU504 4.2 66.5 1.0
CA B:CYS559 4.3 54.8 1.0
CE1 B:TYR533 4.5 69.8 1.0
CD1 B:TRP570 4.6 54.4 1.0
N B:THR558 4.7 56.6 1.0
SG B:CYS556 4.7 66.8 1.0
SG B:CYS528 4.8 53.4 1.0
SG B:CYS553 4.8 69.5 1.0
CZ B:TYR533 4.8 69.4 1.0
N B:LYS557 4.9 60.0 1.0

Reference:

J.Zhang, F.E.Frerman, J.J.Kim. Structure of Electron Transfer Flavoprotein-Ubiquinone Oxidoreductase and Electron Transfer to the Mitochondrial Ubiquinone Pool. Proc.Natl.Acad.Sci.Usa V. 103 16212 2006.
ISSN: ISSN 0027-8424
PubMed: 17050691
DOI: 10.1073/PNAS.0604567103
Page generated: Sat Aug 3 22:34:58 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy