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Iron in PDB 5epa: Crystal Structure of Non-Heme Alpha Ketoglutarate Dependent Carbocyclase Snok From Nogalamycin Biosynthesis

Protein crystallography data

The structure of Crystal Structure of Non-Heme Alpha Ketoglutarate Dependent Carbocyclase Snok From Nogalamycin Biosynthesis, PDB code: 5epa was solved by B.Selvaraj, Y.Lindqvist, V.Siitonen, L.Niiranen, M.Metsa-Ketela, G.Schneider, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.70 / 2.24
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 76.009, 83.151, 271.677, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 22.8

Other elements in 5epa:

The structure of Crystal Structure of Non-Heme Alpha Ketoglutarate Dependent Carbocyclase Snok From Nogalamycin Biosynthesis also contains other interesting chemical elements:

Magnesium (Mg) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Non-Heme Alpha Ketoglutarate Dependent Carbocyclase Snok From Nogalamycin Biosynthesis (pdb code 5epa). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 6 binding sites of Iron where determined in the Crystal Structure of Non-Heme Alpha Ketoglutarate Dependent Carbocyclase Snok From Nogalamycin Biosynthesis, PDB code: 5epa:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6;

Iron binding site 1 out of 6 in 5epa

Go back to Iron Binding Sites List in 5epa
Iron binding site 1 out of 6 in the Crystal Structure of Non-Heme Alpha Ketoglutarate Dependent Carbocyclase Snok From Nogalamycin Biosynthesis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Non-Heme Alpha Ketoglutarate Dependent Carbocyclase Snok From Nogalamycin Biosynthesis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:25.1
occ:1.00
O2 A:AKG301 1.9 14.1 1.0
OD1 A:ASP123 1.9 24.4 1.0
NE2 A:HIS121 2.1 24.5 1.0
O5 A:AKG301 2.1 16.3 1.0
NE2 A:HIS210 2.1 26.2 1.0
O A:HOH477 2.2 21.0 1.0
C1 A:AKG301 2.8 13.4 1.0
C2 A:AKG301 2.9 13.7 1.0
CE1 A:HIS210 3.0 25.1 1.0
CG A:ASP123 3.0 22.6 1.0
CE1 A:HIS121 3.1 23.6 1.0
CD2 A:HIS121 3.1 23.4 1.0
CD2 A:HIS210 3.3 24.9 1.0
OD2 A:ASP123 3.5 21.4 1.0
O A:HOH492 3.9 16.9 1.0
O1 A:AKG301 4.0 14.6 1.0
O A:HOH562 4.1 37.1 1.0
ND1 A:HIS210 4.2 25.0 1.0
ND1 A:HIS121 4.2 23.1 1.0
CG A:HIS121 4.2 23.2 1.0
NE2 A:HIS204 4.3 22.7 1.0
O A:HOH560 4.3 37.8 1.0
O A:HOH557 4.3 23.1 1.0
C3 A:AKG301 4.3 13.2 1.0
CG A:HIS210 4.3 24.3 1.0
CB A:ASP123 4.4 23.2 1.0
CH2 A:TRP57 4.6 26.8 1.0
CA A:ASP123 4.7 23.6 1.0
CE1 A:HIS204 4.9 22.2 1.0
N A:ASP123 5.0 22.7 1.0

Iron binding site 2 out of 6 in 5epa

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Iron binding site 2 out of 6 in the Crystal Structure of Non-Heme Alpha Ketoglutarate Dependent Carbocyclase Snok From Nogalamycin Biosynthesis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Non-Heme Alpha Ketoglutarate Dependent Carbocyclase Snok From Nogalamycin Biosynthesis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe301

b:22.5
occ:1.00
O1 B:AKG302 1.9 14.4 1.0
OD1 B:ASP123 2.0 24.5 1.0
O5 B:AKG302 2.1 14.7 1.0
NE2 B:HIS121 2.1 26.5 1.0
NE2 B:HIS210 2.1 24.4 1.0
O B:HOH454 2.1 21.2 1.0
C1 B:AKG302 2.8 14.5 1.0
C2 B:AKG302 2.8 13.8 1.0
CE1 B:HIS210 2.9 23.1 1.0
CE1 B:HIS121 3.0 25.9 1.0
CG B:ASP123 3.1 22.2 1.0
CD2 B:HIS121 3.1 26.5 1.0
CD2 B:HIS210 3.3 23.1 1.0
OD2 B:ASP123 3.5 20.7 1.0
O2 B:AKG302 4.1 13.4 1.0
ND1 B:HIS210 4.1 23.0 1.0
ND1 B:HIS121 4.1 26.4 1.0
O B:HOH514 4.2 35.3 1.0
O B:HOH455 4.2 19.1 1.0
O B:HOH503 4.2 35.4 1.0
CG B:HIS121 4.2 26.5 1.0
NE2 B:HIS204 4.3 22.9 1.0
CG B:HIS210 4.3 22.2 1.0
C3 B:AKG302 4.3 12.8 1.0
CB B:ASP123 4.5 23.4 1.0
CH2 B:TRP57 4.6 30.6 1.0
CA B:ASP123 4.8 25.3 1.0
CE1 B:HIS204 4.9 22.5 1.0
N B:ASP123 4.9 24.7 1.0
C4 B:AKG302 5.0 12.2 1.0

Iron binding site 3 out of 6 in 5epa

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Iron binding site 3 out of 6 in the Crystal Structure of Non-Heme Alpha Ketoglutarate Dependent Carbocyclase Snok From Nogalamycin Biosynthesis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Non-Heme Alpha Ketoglutarate Dependent Carbocyclase Snok From Nogalamycin Biosynthesis within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe300

b:25.6
occ:1.00
OD1 C:ASP123 1.9 27.3 1.0
O2 C:AKG301 1.9 14.2 1.0
O C:HOH449 2.1 24.1 1.0
O5 C:AKG301 2.1 14.5 1.0
NE2 C:HIS121 2.1 25.2 1.0
NE2 C:HIS210 2.1 25.7 1.0
C1 C:AKG301 2.8 13.4 1.0
C2 C:AKG301 2.8 13.2 1.0
CE1 C:HIS210 2.9 24.8 1.0
CG C:ASP123 3.0 26.7 1.0
CE1 C:HIS121 3.1 23.9 1.0
CD2 C:HIS121 3.1 23.9 1.0
CD2 C:HIS210 3.3 24.0 1.0
OD2 C:ASP123 3.4 27.9 1.0
O C:HOH524 3.9 35.5 1.0
O1 C:AKG301 4.1 13.4 1.0
O C:HOH463 4.1 21.7 1.0
ND1 C:HIS210 4.1 24.9 1.0
ND1 C:HIS121 4.2 23.9 1.0
O C:HOH553 4.2 39.6 1.0
CG C:HIS121 4.2 24.2 1.0
NE2 C:HIS204 4.2 22.9 1.0
C3 C:AKG301 4.3 12.9 1.0
CB C:ASP123 4.3 27.2 1.0
CG C:HIS210 4.3 23.9 1.0
CA C:ASP123 4.7 27.9 1.0
CH2 C:TRP57 4.7 25.1 1.0
CE1 C:HIS204 4.8 22.7 1.0
N C:ASP123 4.9 26.2 1.0
C4 C:AKG301 5.0 12.2 1.0

Iron binding site 4 out of 6 in 5epa

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Iron binding site 4 out of 6 in the Crystal Structure of Non-Heme Alpha Ketoglutarate Dependent Carbocyclase Snok From Nogalamycin Biosynthesis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Non-Heme Alpha Ketoglutarate Dependent Carbocyclase Snok From Nogalamycin Biosynthesis within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe301

b:27.1
occ:1.00
O2 D:AKG302 1.9 18.4 1.0
OD1 D:ASP123 2.0 23.4 1.0
NE2 D:HIS121 2.1 25.6 1.0
O5 D:AKG302 2.1 17.1 1.0
O D:HOH445 2.1 25.9 1.0
NE2 D:HIS210 2.1 26.6 1.0
C1 D:AKG302 2.8 17.1 1.0
C2 D:AKG302 2.9 16.1 1.0
CE1 D:HIS210 3.0 26.2 1.0
CE1 D:HIS121 3.0 24.6 1.0
CG D:ASP123 3.1 22.8 1.0
CD2 D:HIS121 3.1 24.4 1.0
CD2 D:HIS210 3.3 25.4 1.0
OD2 D:ASP123 3.5 21.5 1.0
O1 D:AKG302 4.0 18.3 1.0
ND1 D:HIS121 4.1 24.6 1.0
ND1 D:HIS210 4.2 26.5 1.0
CG D:HIS121 4.2 24.2 1.0
O D:HOH472 4.2 20.8 1.0
NE2 D:HIS204 4.3 27.0 1.0
O D:HOH564 4.3 31.1 1.0
CG D:HIS210 4.4 25.9 1.0
C3 D:AKG302 4.4 14.5 1.0
O D:HOH560 4.4 29.2 1.0
CB D:ASP123 4.4 23.9 1.0
CH2 D:TRP57 4.6 22.9 1.0
CA D:ASP123 4.8 24.7 1.0
CE1 D:HIS204 4.9 26.7 1.0
N D:ASP123 4.9 23.5 1.0

Iron binding site 5 out of 6 in 5epa

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Iron binding site 5 out of 6 in the Crystal Structure of Non-Heme Alpha Ketoglutarate Dependent Carbocyclase Snok From Nogalamycin Biosynthesis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Crystal Structure of Non-Heme Alpha Ketoglutarate Dependent Carbocyclase Snok From Nogalamycin Biosynthesis within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe300

b:23.2
occ:1.00
O1 E:AKG301 1.9 14.5 1.0
OD1 E:ASP123 1.9 21.1 1.0
NE2 E:HIS121 2.1 21.5 1.0
O5 E:AKG301 2.1 15.2 1.0
O E:HOH443 2.1 19.8 1.0
NE2 E:HIS210 2.1 24.8 1.0
C1 E:AKG301 2.8 14.6 1.0
C2 E:AKG301 2.9 13.6 1.0
CE1 E:HIS210 2.9 23.8 1.0
CG E:ASP123 3.0 19.0 1.0
CE1 E:HIS121 3.1 20.4 1.0
CD2 E:HIS121 3.1 20.8 1.0
CD2 E:HIS210 3.3 23.1 1.0
OD2 E:ASP123 3.4 18.4 1.0
O2 E:AKG301 4.0 14.9 1.0
O E:HOH572 4.1 38.4 1.0
ND1 E:HIS210 4.1 23.9 1.0
ND1 E:HIS121 4.2 20.7 1.0
O E:HOH567 4.2 23.9 1.0
O E:HOH442 4.2 22.4 1.0
NE2 E:HIS204 4.2 20.2 1.0
CG E:HIS121 4.2 20.8 1.0
O E:HOH573 4.3 30.5 1.0
CB E:ASP123 4.3 20.0 1.0
CG E:HIS210 4.3 22.6 1.0
C3 E:AKG301 4.4 12.9 1.0
CH2 E:TRP57 4.7 25.7 1.0
CA E:ASP123 4.7 20.7 1.0
CE1 E:HIS204 4.8 21.0 1.0
N E:ASP123 4.9 20.8 1.0

Iron binding site 6 out of 6 in 5epa

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Iron binding site 6 out of 6 in the Crystal Structure of Non-Heme Alpha Ketoglutarate Dependent Carbocyclase Snok From Nogalamycin Biosynthesis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Crystal Structure of Non-Heme Alpha Ketoglutarate Dependent Carbocyclase Snok From Nogalamycin Biosynthesis within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe300

b:21.5
occ:1.00
O1 F:AKG301 1.9 15.4 1.0
OD1 F:ASP123 2.0 30.4 1.0
NE2 F:HIS121 2.1 31.6 1.0
O5 F:AKG301 2.1 14.6 1.0
NE2 F:HIS210 2.1 29.4 1.0
O F:HOH434 2.1 26.2 1.0
C1 F:AKG301 2.8 14.5 1.0
C2 F:AKG301 2.9 14.3 1.0
CE1 F:HIS210 2.9 28.6 1.0
CG F:ASP123 3.1 28.2 1.0
CE1 F:HIS121 3.1 30.8 1.0
CD2 F:HIS121 3.1 31.3 1.0
CD2 F:HIS210 3.3 28.0 1.0
OD2 F:ASP123 3.5 28.1 1.0
O2 F:AKG301 4.0 15.1 1.0
ND1 F:HIS210 4.1 28.4 1.0
O F:HOH457 4.2 22.4 1.0
ND1 F:HIS121 4.2 31.0 1.0
CG F:HIS121 4.2 31.4 1.0
NE2 F:HIS204 4.3 26.6 1.0
CG F:HIS210 4.3 27.5 1.0
C3 F:AKG301 4.4 14.2 1.0
CB F:ASP123 4.4 28.8 1.0
O F:HOH487 4.5 27.9 1.0
CH2 F:TRP57 4.6 38.5 1.0
CA F:ASP123 4.7 29.7 1.0
CE1 F:HIS204 4.9 26.0 1.0
N F:ASP123 4.9 29.3 1.0
C4 F:AKG301 4.9 13.9 1.0

Reference:

V.Siitonen, B.Selvaraj, L.Niiranen, Y.Lindqvist, G.Schneider, M.Metsa-Ketela. Divergent Non-Heme Iron Enzymes in the Nogalamycin Biosynthetic Pathway. Proc.Natl.Acad.Sci.Usa V. 113 5251 2016.
ISSN: ESSN 1091-6490
PubMed: 27114534
DOI: 10.1073/PNAS.1525034113
Page generated: Sun Dec 13 16:00:44 2020

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