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Iron in PDB 6f6d: The Catalytic Domain of KDM6B in Complex with H3(17-33)K18IA21M Peptide

Protein crystallography data

The structure of The Catalytic Domain of KDM6B in Complex with H3(17-33)K18IA21M Peptide, PDB code: 6f6d was solved by S.E.Jones, L.Olsen, M.Gajhede, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 57.50 / 1.82
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 68.480, 68.480, 230.000, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 21.4

Other elements in 6f6d:

The structure of The Catalytic Domain of KDM6B in Complex with H3(17-33)K18IA21M Peptide also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the The Catalytic Domain of KDM6B in Complex with H3(17-33)K18IA21M Peptide (pdb code 6f6d). 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 The Catalytic Domain of KDM6B in Complex with H3(17-33)K18IA21M Peptide, PDB code: 6f6d:

Iron binding site 1 out of 1 in 6f6d

Go back to Iron Binding Sites List in 6f6d
Iron binding site 1 out of 1 in the The Catalytic Domain of KDM6B in Complex with H3(17-33)K18IA21M Peptide


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Catalytic Domain of KDM6B in Complex with H3(17-33)K18IA21M Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1701

b:23.9
occ:1.00
OE2 A:GLU1392 2.0 23.6 1.0
NE2 A:HIS1470 2.1 20.4 1.0
O2 A:AKG1703 2.1 23.4 1.0
NE2 A:HIS1390 2.2 19.6 1.0
O5 A:AKG1703 2.2 26.6 1.0
O A:HOH2098 2.3 28.8 1.0
C1 A:AKG1703 2.8 35.8 1.0
C2 A:AKG1703 2.8 32.3 1.0
CE1 A:HIS1470 3.0 21.9 1.0
CE1 A:HIS1390 3.0 22.1 1.0
CD A:GLU1392 3.1 21.7 1.0
HE1 A:HIS1470 3.1 26.3 1.0
HE1 A:HIS1390 3.1 26.5 1.0
CD2 A:HIS1470 3.2 20.0 1.0
CD2 A:HIS1390 3.2 25.1 1.0
HD2 A:HIS1470 3.4 24.0 1.0
HD2 A:HIS1390 3.5 30.1 1.0
OE1 A:GLU1392 3.6 22.6 1.0
HG A:SER1398 3.8 36.2 1.0
O1 A:AKG1703 4.0 27.1 1.0
ND1 A:HIS1470 4.1 21.0 1.0
ND1 A:HIS1390 4.2 21.4 1.0
C3 A:AKG1703 4.2 41.2 1.0
CG A:HIS1470 4.3 18.7 1.0
HG2 A:GLU1392 4.3 22.4 1.0
CG A:GLU1392 4.3 18.7 1.0
O A:HOH2157 4.3 41.6 1.0
CG A:HIS1390 4.3 21.9 1.0
O A:HOH1815 4.4 37.9 1.0
H32 A:AKG1703 4.4 49.5 1.0
HB2 A:SER1398 4.5 30.6 1.0
OG A:SER1398 4.5 30.1 1.0
HG21 A:THR1387 4.6 29.2 1.0
HZ3 B:LYS27 4.6 48.6 1.0
HB3 A:SER1398 4.7 30.6 1.0
O A:HOH2146 4.7 42.4 1.0
H31 A:AKG1703 4.7 49.5 1.0
HG3 A:GLU1392 4.8 22.4 1.0
HD13 A:ILE1464 4.8 31.8 1.0
CB A:SER1398 4.8 25.5 1.0
HA A:GLU1392 4.8 25.3 1.0
HD1 A:HIS1470 4.9 25.2 1.0
HZ3 A:TRP1410 4.9 28.5 1.0
H41 A:AKG1703 4.9 51.1 1.0
HD1 A:HIS1390 4.9 25.7 1.0
HG21 A:ILE1464 5.0 26.8 1.0
HG12 A:ILE1464 5.0 31.2 1.0

Reference:

S.E.Jones, L.Olsen, M.Gajhede. Structural Basis of Histone Demethylase KDM6B Histone 3 Lysine 27 Specificity. Biochemistry V. 57 585 2018.
ISSN: ISSN 1520-4995
PubMed: 29220567
DOI: 10.1021/ACS.BIOCHEM.7B01152
Page generated: Wed Aug 6 05:58:14 2025

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