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Iron in PDB 1olt: Coproporphyrinogen III Oxidase (Hemn) From Escherichia Coli Is A Radical Sam Enzyme.

Protein crystallography data

The structure of Coproporphyrinogen III Oxidase (Hemn) From Escherichia Coli Is A Radical Sam Enzyme., PDB code: 1olt was solved by G.Layer, J.Moser, D.W.Heinz, D.Jahn, W.-D.Schubert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100.00 / 2.07
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 114.036, 114.036, 76.459, 90.00, 90.00, 120.00
R / Rfree (%) 15.4 / 18.7

Iron Binding Sites:

The binding sites of Iron atom in the Coproporphyrinogen III Oxidase (Hemn) From Escherichia Coli Is A Radical Sam Enzyme. (pdb code 1olt). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Coproporphyrinogen III Oxidase (Hemn) From Escherichia Coli Is A Radical Sam Enzyme., PDB code: 1olt:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1olt

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Iron binding site 1 out of 4 in the Coproporphyrinogen III Oxidase (Hemn) From Escherichia Coli Is A Radical Sam Enzyme.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Coproporphyrinogen III Oxidase (Hemn) From Escherichia Coli Is A Radical Sam Enzyme. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:23.8
occ:1.00
FE1 A:SF4500 0.0 23.8 1.0
S3 A:SF4500 2.1 15.2 1.0
S4 A:SF4500 2.2 17.1 1.0
S2 A:SF4500 2.2 13.4 1.0
SG A:CYS62 2.3 12.6 1.0
FE4 A:SF4500 2.5 28.0 1.0
FE3 A:SF4500 2.5 28.9 1.0
FE2 A:SF4500 2.7 25.7 1.0
CB A:CYS62 3.2 12.7 1.0
OG1 A:THR114 3.8 14.9 1.0
S1 A:SF4500 3.9 15.0 1.0
N A:SAM501 3.9 18.7 1.0
CG A:LYS73 4.1 12.3 0.3
CD A:LYS73 4.4 13.5 0.3
O A:HOH2066 4.4 17.8 1.0
O A:SAM501 4.5 18.8 1.0
CG A:LYS73 4.6 14.0 0.7
CD A:LYS73 4.6 16.8 0.7
CA A:CYS62 4.6 12.3 1.0
CB A:LYS73 4.6 12.9 0.3
O A:LYS64 4.7 13.2 1.0
CB A:LYS73 4.7 13.4 0.7
C A:GLY113 4.7 12.8 1.0
CA A:GLY113 4.7 13.2 1.0
SG A:CYS69 4.7 15.6 1.0
SG A:CYS66 4.7 13.7 1.0
O A:HOH2132 4.8 13.4 1.0
CE A:LYS73 4.9 17.1 0.7
O A:GLY113 4.9 14.0 1.0
NZ A:LYS73 5.0 13.1 0.3

Iron binding site 2 out of 4 in 1olt

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Iron binding site 2 out of 4 in the Coproporphyrinogen III Oxidase (Hemn) From Escherichia Coli Is A Radical Sam Enzyme.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Coproporphyrinogen III Oxidase (Hemn) From Escherichia Coli Is A Radical Sam Enzyme. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:25.7
occ:1.00
FE2 A:SF4500 0.0 25.7 1.0
S4 A:SF4500 2.1 17.1 1.0
S3 A:SF4500 2.2 15.2 1.0
S1 A:SF4500 2.2 15.0 1.0
SG A:CYS69 2.4 15.6 1.0
FE4 A:SF4500 2.4 28.0 1.0
FE3 A:SF4500 2.6 28.9 1.0
FE1 A:SF4500 2.7 23.8 1.0
CB A:CYS69 3.1 13.8 1.0
S2 A:SF4500 3.9 13.4 1.0
NZ A:LYS73 4.0 13.1 0.3
CG A:LYS73 4.2 12.3 0.3
SG A:CYS71 4.2 9.6 0.5
CG A:LYS73 4.5 14.0 0.7
O A:SAM501 4.5 18.8 1.0
CA A:CYS69 4.5 12.8 1.0
SD A:SAM501 4.5 19.9 0.6
CB A:CYS66 4.6 10.4 1.0
SG A:CYS66 4.6 13.7 1.0
CB A:CYS71 4.6 12.4 0.5
CB A:CYS71 4.6 10.9 0.5
SG A:CYS62 4.7 12.6 1.0
CE A:LYS73 4.7 17.1 0.7
CD A:LYS73 4.7 13.5 0.3
N A:SAM501 4.8 18.7 1.0
CD A:LYS73 4.9 16.8 0.7
CE1 A:PHE68 4.9 14.3 1.0

Iron binding site 3 out of 4 in 1olt

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Iron binding site 3 out of 4 in the Coproporphyrinogen III Oxidase (Hemn) From Escherichia Coli Is A Radical Sam Enzyme.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Coproporphyrinogen III Oxidase (Hemn) From Escherichia Coli Is A Radical Sam Enzyme. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:28.9
occ:1.00
FE3 A:SF4500 0.0 28.9 1.0
S4 A:SF4500 2.2 17.1 1.0
O A:SAM501 2.2 18.8 1.0
S1 A:SF4500 2.3 15.0 1.0
S2 A:SF4500 2.3 13.4 1.0
FE4 A:SF4500 2.4 28.0 1.0
FE1 A:SF4500 2.5 23.8 1.0
N A:SAM501 2.5 18.7 1.0
FE2 A:SF4500 2.6 25.7 1.0
C A:SAM501 3.1 19.3 1.0
CA A:SAM501 3.3 18.1 1.0
SD A:SAM501 3.5 19.9 0.6
S3 A:SF4500 3.6 15.2 1.0
CG A:SAM501 3.7 18.9 0.4
NH1 A:ARG184 4.1 14.7 1.0
CB A:SAM501 4.1 20.0 1.0
CG A:SAM501 4.1 20.9 0.6
CE A:SAM501 4.3 22.1 0.6
OXT A:SAM501 4.3 17.5 1.0
OG1 A:THR114 4.3 14.9 1.0
SG A:CYS62 4.4 12.6 1.0
O A:GLY113 4.6 14.0 1.0
SG A:CYS66 4.6 13.7 1.0
SG A:CYS69 4.8 15.6 1.0

Iron binding site 4 out of 4 in 1olt

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Iron binding site 4 out of 4 in the Coproporphyrinogen III Oxidase (Hemn) From Escherichia Coli Is A Radical Sam Enzyme.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Coproporphyrinogen III Oxidase (Hemn) From Escherichia Coli Is A Radical Sam Enzyme. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:28.0
occ:1.00
FE4 A:SF4500 0.0 28.0 1.0
S3 A:SF4500 2.1 15.2 1.0
S2 A:SF4500 2.2 13.4 1.0
S1 A:SF4500 2.3 15.0 1.0
FE3 A:SF4500 2.4 28.9 1.0
FE2 A:SF4500 2.4 25.7 1.0
FE1 A:SF4500 2.5 23.8 1.0
SG A:CYS66 2.5 13.7 1.0
CB A:CYS66 3.3 10.4 1.0
S4 A:SF4500 3.5 17.1 1.0
O A:SAM501 3.7 18.8 1.0
NH1 A:ARG184 3.8 14.7 1.0
NH2 A:ARG149 4.3 14.6 1.0
O A:HOH2066 4.4 17.8 1.0
N A:CYS66 4.4 11.1 1.0
CB A:CYS69 4.4 13.8 1.0
CA A:CYS66 4.5 11.3 1.0
SG A:CYS69 4.5 15.6 1.0
O A:LYS64 4.6 13.2 1.0
N A:SAM501 4.7 18.7 1.0
CZ A:PHE68 4.7 14.6 1.0
SG A:CYS62 4.7 12.6 1.0
C A:SAM501 4.8 19.3 1.0

Reference:

G.Layer, J.Moser, D.W.Heinz, D.Jahn, W.-D.Schubert. Crystal Structure of Coproporphyrinogen III Oxidase Reveals Cofactor Geometry of Radical Sam Enzymes Embo J. V. 22 6214 2003.
ISSN: ISSN 0261-4189
PubMed: 14633981
DOI: 10.1093/EMBOJ/CDG598
Page generated: Sat Aug 3 12:31:51 2024

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