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Iron in PDB 5o0t: Crystal Structure of Trans-Membrane Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5)

Protein crystallography data

The structure of Crystal Structure of Trans-Membrane Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5), PDB code: 5o0t was solved by F.Magnani, S.Nenci, A.Mattevi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.60 / 2.05
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.371, 74.570, 85.120, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 22.1

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Trans-Membrane Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5) (pdb code 5o0t). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Trans-Membrane Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5), PDB code: 5o0t:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 5o0t

Go back to Iron Binding Sites List in 5o0t
Iron binding site 1 out of 2 in the Crystal Structure of Trans-Membrane Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5)


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 Trans-Membrane Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe504

b:24.3
occ:1.00
FE A:HEM504 0.0 24.3 1.0
ND A:HEM504 1.9 26.0 1.0
NA A:HEM504 2.0 25.8 1.0
NE2 A:HIS299 2.0 25.1 1.0
NE2 A:HIS372 2.0 25.4 1.0
NB A:HEM504 2.1 27.2 1.0
NC A:HEM504 2.1 25.1 1.0
C1D A:HEM504 2.9 26.6 1.0
C4D A:HEM504 2.9 26.3 1.0
CE1 A:HIS372 2.9 24.4 1.0
CE1 A:HIS299 3.0 24.2 1.0
C4A A:HEM504 3.0 27.6 1.0
C1A A:HEM504 3.0 26.3 1.0
CD2 A:HIS299 3.0 24.3 1.0
C4B A:HEM504 3.0 26.4 1.0
C1B A:HEM504 3.0 27.6 1.0
C4C A:HEM504 3.1 26.2 1.0
CD2 A:HIS372 3.1 25.9 1.0
C1C A:HEM504 3.1 25.0 1.0
CHD A:HEM504 3.4 25.8 1.0
CHB A:HEM504 3.4 25.9 1.0
CHA A:HEM504 3.4 25.4 1.0
CHC A:HEM504 3.5 25.8 1.0
ND1 A:HIS372 4.1 26.1 1.0
ND1 A:HIS299 4.1 22.6 1.0
C2D A:HEM504 4.2 27.7 1.0
CG A:HIS299 4.2 24.1 1.0
C3D A:HEM504 4.2 29.8 1.0
CG A:HIS372 4.2 27.0 1.0
C3A A:HEM504 4.2 29.7 1.0
C2A A:HEM504 4.2 31.4 1.0
C2B A:HEM504 4.3 27.6 1.0
C3B A:HEM504 4.3 30.8 1.0
C3C A:HEM504 4.3 28.0 1.0
C2C A:HEM504 4.3 27.4 1.0

Iron binding site 2 out of 2 in 5o0t

Go back to Iron Binding Sites List in 5o0t
Iron binding site 2 out of 2 in the Crystal Structure of Trans-Membrane Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5)


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 Trans-Membrane Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe505

b:23.5
occ:1.00
FE A:HEM505 0.0 23.5 1.0
NE2 A:HIS385 1.9 26.0 1.0
ND A:HEM505 1.9 24.8 1.0
NE2 A:HIS313 2.0 25.0 1.0
NA A:HEM505 2.0 24.7 1.0
NC A:HEM505 2.1 24.8 1.0
NB A:HEM505 2.1 24.0 1.0
CE1 A:HIS385 2.9 25.8 1.0
CE1 A:HIS313 3.0 23.7 1.0
C1D A:HEM505 3.0 24.9 1.0
C4D A:HEM505 3.0 24.2 1.0
CD2 A:HIS385 3.0 25.4 1.0
C1A A:HEM505 3.0 25.0 1.0
CD2 A:HIS313 3.0 23.7 1.0
C4B A:HEM505 3.0 25.2 1.0
C4C A:HEM505 3.1 24.3 1.0
C4A A:HEM505 3.1 26.6 1.0
C1B A:HEM505 3.1 25.4 1.0
C1C A:HEM505 3.1 24.8 1.0
CHA A:HEM505 3.4 23.5 1.0
CHD A:HEM505 3.4 22.3 1.0
CHC A:HEM505 3.4 22.8 1.0
CHB A:HEM505 3.5 25.0 1.0
ND1 A:HIS385 4.0 24.1 1.0
ND1 A:HIS313 4.1 23.2 1.0
CG A:HIS385 4.1 25.2 1.0
CG A:HIS313 4.1 23.2 1.0
C2A A:HEM505 4.2 26.6 1.0
C2D A:HEM505 4.2 24.6 1.0
C3D A:HEM505 4.3 27.4 1.0
C3A A:HEM505 4.3 26.1 1.0
C3C A:HEM505 4.3 25.3 1.0
C2C A:HEM505 4.3 24.3 1.0
C2B A:HEM505 4.3 25.4 1.0
C3B A:HEM505 4.3 25.5 1.0
CD2 A:HIS317 4.6 25.4 1.0
NE2 A:HIS317 4.7 25.3 1.0

Reference:

F.Magnani, S.Nenci, E.Millana Fananas, M.Ceccon, E.Romero, M.W.Fraaije, A.Mattevi. Crystal Structures and Atomic Model of Nadph Oxidase. Proc. Natl. Acad. Sci. V. 114 6764 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28607049
DOI: 10.1073/PNAS.1702293114
Page generated: Tue Aug 6 06:20:15 2024

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