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Iron in PDB 7fcb: Sptf 9 Residues Truncated Mutant

Protein crystallography data

The structure of Sptf 9 Residues Truncated Mutant, PDB code: 7fcb was solved by T.Hui, T.Mori, I.Abe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.10 / 1.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.21, 52.316, 57.784, 90, 99.44, 90
R / Rfree (%) 16.9 / 19.6

Iron Binding Sites:

The binding sites of Iron atom in the Sptf 9 Residues Truncated Mutant (pdb code 7fcb). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Sptf 9 Residues Truncated Mutant, PDB code: 7fcb:

Iron binding site 1 out of 1 in 7fcb

Go back to Iron Binding Sites List in 7fcb
Iron binding site 1 out of 1 in the Sptf 9 Residues Truncated Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Sptf 9 Residues Truncated Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe302

b:11.3
occ:1.00
O2' C:OGA301 2.1 12.2 1.0
NE2 C:HIS196 2.1 10.7 1.0
O2 C:OGA301 2.2 13.3 1.0
O C:HOH421 2.2 12.6 1.0
OD1 C:ASP121 2.2 10.9 1.0
NE2 C:HIS119 2.2 13.4 1.0
C2 C:OGA301 2.8 12.1 1.0
C1 C:OGA301 2.9 14.5 1.0
CE1 C:HIS196 3.0 12.6 1.0
CE1 C:HIS119 3.1 12.9 1.0
CG C:ASP121 3.1 10.9 1.0
CD2 C:HIS196 3.1 11.0 1.0
CD2 C:HIS119 3.2 12.7 1.0
OD2 C:ASP121 3.4 11.5 1.0
O C:HOH580 3.9 21.8 1.0
O1 C:OGA301 4.1 15.9 1.0
N1 C:OGA301 4.1 13.2 1.0
ND1 C:HIS196 4.2 10.9 1.0
CG C:HIS196 4.2 9.7 1.0
ND1 C:HIS119 4.2 13.2 1.0
O C:HOH487 4.3 16.0 1.0
CG C:HIS119 4.3 10.9 1.0
O C:HOH477 4.3 25.5 1.0
CB C:ASP121 4.5 10.5 1.0
O C:HOH586 4.7 19.4 1.0
C4 C:OGA301 4.8 13.6 1.0
CA C:ASP121 4.9 10.3 1.0

Reference:

H.Tao, T.Mori, H.Chen, S.Lyu, A.Nonoyama, S.Lee, I.Abe. Molecular Insights Into the Unusually Promiscuous and Catalytically Versatile Fe(II)/ Alpha-Ketoglutarate-Dependent Oxygenase Sptf. Nat Commun V. 13 95 2022.
ISSN: ESSN 2041-1723
PubMed: 35013177
DOI: 10.1038/S41467-021-27636-3
Page generated: Wed Apr 5 02:56:07 2023

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