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Iron in PDB 3k3n: Crystal Structure of the Catalytic Core Domain of Human PHF8

Protein crystallography data

The structure of Crystal Structure of the Catalytic Core Domain of Human PHF8, PDB code: 3k3n was solved by L.Yu, Y.Wang, S.Huang, J.Wang, Z.Deng, W.Wu, W.Gong, Z.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.238, 52.583, 134.930, 90.00, 90.00, 90.00
R / Rfree (%) 22.2 / 26.1

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Catalytic Core Domain of Human PHF8 (pdb code 3k3n). 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 Crystal Structure of the Catalytic Core Domain of Human PHF8, PDB code: 3k3n:

Iron binding site 1 out of 1 in 3k3n

Go back to Iron Binding Sites List in 3k3n
Iron binding site 1 out of 1 in the Crystal Structure of the Catalytic Core Domain of Human PHF8


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 the Catalytic Core Domain of Human PHF8 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1

b:39.1
occ:1.00
OD1 A:ASP249 2.1 32.4 1.0
O A:HOH19 2.1 33.8 1.0
NE2 A:HIS319 2.1 26.1 1.0
NE2 A:HIS247 2.2 28.2 1.0
O A:HOH8 2.3 40.7 1.0
O A:HOH43 2.5 47.0 1.0
CG A:ASP249 3.1 31.1 1.0
CD2 A:HIS319 3.1 25.6 1.0
CE1 A:HIS319 3.1 25.8 1.0
CE1 A:HIS247 3.1 27.7 1.0
CD2 A:HIS247 3.2 27.0 1.0
OD2 A:ASP249 3.3 34.0 1.0
O A:HOH52 4.1 53.8 1.0
ND1 A:HIS319 4.2 24.6 1.0
CG A:HIS319 4.2 25.4 1.0
ND1 A:HIS247 4.2 27.8 1.0
CG A:HIS247 4.3 27.4 1.0
CB A:ASP249 4.4 29.0 1.0
CA A:ASP249 4.9 28.5 1.0
N A:ASP249 5.0 28.3 1.0

Reference:

L.Yu, Y.Wang, S.Huang, J.Wang, Z.Deng, Q.Zhang, W.Wu, X.Zhang, Z.Liu, W.Gong, Z.Chen. Structural Insights Into A Novel Histone Demethylase PHF8 Cell Res. V. 20 166 2010.
ISSN: ISSN 1001-0602
PubMed: 20101266
DOI: 10.1038/CR.2010.8
Page generated: Tue Aug 5 03:08:36 2025

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