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Iron in PDB 6ojw: Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda

Enzymatic activity of Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda

All present enzymatic activity of Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda:
1.13.11.43;

Protein crystallography data

The structure of Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda, PDB code: 6ojw was solved by E.Kuatsjah, M.M.Verstraete, M.J.Kobylarz, A.K.N.Liu, M.E.P.Murphy, L.D.Eltis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 79.35 / 2.60
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 183.259, 183.259, 95.081, 90.00, 90.00, 120.00
R / Rfree (%) 18.7 / 21.5

Other elements in 6ojw:

The structure of Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda (pdb code 6ojw). 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 Sphingomonas Paucimobilis TMY1009 Holo-Lsda, PDB code: 6ojw:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 6ojw

Go back to Iron Binding Sites List in 6ojw
Iron binding site 1 out of 2 in the Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda


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 Sphingomonas Paucimobilis TMY1009 Holo-Lsda within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:34.1
occ:1.00
NE2 B:HIS218 2.0 39.0 1.0
NE2 B:HIS472 2.1 35.5 1.0
NE2 B:HIS282 2.2 32.8 1.0
NE2 B:HIS167 2.3 26.1 1.0
O B:HOH752 2.5 29.4 1.0
CE1 B:HIS218 2.7 36.8 1.0
HE1 B:HIS218 2.8 44.1 1.0
CD2 B:HIS282 3.0 28.5 1.0
CD2 B:HIS472 3.0 31.6 1.0
CE1 B:HIS472 3.1 26.2 1.0
CE1 B:HIS167 3.1 30.9 1.0
CD2 B:HIS218 3.1 37.4 1.0
HD2 B:HIS282 3.1 34.2 1.0
HE1 B:HIS167 3.2 37.1 1.0
HD2 B:HIS472 3.2 38.0 1.0
CE1 B:HIS282 3.2 35.9 1.0
HE1 B:HIS472 3.3 31.4 1.0
CD2 B:HIS167 3.4 33.7 1.0
HD2 B:HIS218 3.4 44.9 1.0
HE1 B:HIS282 3.5 43.0 1.0
HD2 B:HIS167 3.6 40.5 1.0
HG23 B:THR121 3.8 41.1 1.0
HG21 B:THR121 3.9 41.1 1.0
HG22 B:THR121 3.9 41.1 1.0
ND1 B:HIS218 3.9 32.6 1.0
CG2 B:THR121 4.1 34.2 1.0
CG B:HIS218 4.1 32.2 1.0
ND1 B:HIS472 4.2 22.9 1.0
CG B:HIS472 4.2 26.8 1.0
CG B:HIS282 4.2 37.4 1.0
ND1 B:HIS167 4.3 31.5 1.0
ND1 B:HIS282 4.3 38.9 1.0
CG B:HIS167 4.4 31.6 1.0
HD22 B:LEU471 4.5 35.4 1.0
HD1 B:HIS218 4.7 39.2 1.0
HB3 B:LEU471 4.9 35.6 1.0
HD1 B:HIS472 4.9 27.5 1.0
HE1 B:PHE351 5.0 38.7 1.0

Iron binding site 2 out of 2 in 6ojw

Go back to Iron Binding Sites List in 6ojw
Iron binding site 2 out of 2 in the Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda


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 Sphingomonas Paucimobilis TMY1009 Holo-Lsda within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:38.2
occ:1.00
NE2 A:HIS218 2.0 49.9 1.0
NE2 A:HIS472 2.1 38.5 1.0
NE2 A:HIS282 2.2 32.8 1.0
NE2 A:HIS167 2.4 34.1 1.0
O A:HOH741 2.5 34.0 1.0
CE1 A:HIS218 2.7 44.2 1.0
HE1 A:HIS218 2.8 53.0 1.0
CE1 A:HIS472 3.0 34.6 1.0
CD2 A:HIS472 3.1 31.5 1.0
CD2 A:HIS282 3.1 32.7 1.0
CE1 A:HIS282 3.1 35.9 1.0
CD2 A:HIS218 3.1 40.9 1.0
HE1 A:HIS472 3.2 41.5 1.0
HD2 A:HIS282 3.2 39.3 1.0
HD2 A:HIS472 3.3 37.8 1.0
CE1 A:HIS167 3.3 36.3 1.0
HE1 A:HIS282 3.3 43.0 1.0
HE1 A:HIS167 3.4 43.6 1.0
CD2 A:HIS167 3.4 37.4 1.0
HD2 A:HIS218 3.5 49.1 1.0
HD2 A:HIS167 3.6 44.9 1.0
HG23 A:THR121 3.9 48.3 1.0
ND1 A:HIS218 3.9 40.7 1.0
HG22 A:THR121 4.1 48.3 1.0
HG21 A:THR121 4.1 48.3 1.0
ND1 A:HIS472 4.1 30.4 1.0
CG A:HIS218 4.1 40.3 1.0
CG A:HIS472 4.2 27.9 1.0
ND1 A:HIS282 4.2 31.4 1.0
CG A:HIS282 4.2 32.9 1.0
CG2 A:THR121 4.3 40.2 1.0
ND1 A:HIS167 4.4 36.4 1.0
CG A:HIS167 4.5 35.3 1.0
HD22 A:LEU471 4.6 41.1 1.0
HD1 A:HIS218 4.7 48.9 1.0
HB3 A:LEU471 4.9 39.0 1.0
HE1 A:PHE351 4.9 39.5 1.0
HD1 A:HIS472 4.9 36.5 1.0
HD1 A:HIS282 5.0 37.7 1.0

Reference:

E.Kuatsjah, M.M.Verstraete, M.J.Kobylarz, A.K.N.Liu, M.E.P.Murphy, L.D.Eltis. Identification of Functionally Important Residues and Structural Features in A Bacterial Lignostilbene Dioxygenase. J.Biol.Chem. V. 294 12911 2019.
ISSN: ESSN 1083-351X
PubMed: 31292192
DOI: 10.1074/JBC.RA119.009428
Page generated: Wed Aug 7 04:26:46 2024

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