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Iron in PDB 2ilm: Factor Inhibiting Hif-1 Alpha D201A Mutant in Complex with Fe(II), Alpha-Ketoglutarate and Hif-1 Alpha 35MER

Enzymatic activity of Factor Inhibiting Hif-1 Alpha D201A Mutant in Complex with Fe(II), Alpha-Ketoglutarate and Hif-1 Alpha 35MER

All present enzymatic activity of Factor Inhibiting Hif-1 Alpha D201A Mutant in Complex with Fe(II), Alpha-Ketoglutarate and Hif-1 Alpha 35MER:
1.14.11.16;

Protein crystallography data

The structure of Factor Inhibiting Hif-1 Alpha D201A Mutant in Complex with Fe(II), Alpha-Ketoglutarate and Hif-1 Alpha 35MER, PDB code: 2ilm was solved by M.A.Mcdonough, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.27 / 2.30
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 86.531, 86.531, 147.640, 90.00, 90.00, 90.00
R / Rfree (%) 20.9 / 26.7

Iron Binding Sites:

The binding sites of Iron atom in the Factor Inhibiting Hif-1 Alpha D201A Mutant in Complex with Fe(II), Alpha-Ketoglutarate and Hif-1 Alpha 35MER (pdb code 2ilm). 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 Factor Inhibiting Hif-1 Alpha D201A Mutant in Complex with Fe(II), Alpha-Ketoglutarate and Hif-1 Alpha 35MER, PDB code: 2ilm:

Iron binding site 1 out of 1 in 2ilm

Go back to Iron Binding Sites List in 2ilm
Iron binding site 1 out of 1 in the Factor Inhibiting Hif-1 Alpha D201A Mutant in Complex with Fe(II), Alpha-Ketoglutarate and Hif-1 Alpha 35MER


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Factor Inhibiting Hif-1 Alpha D201A Mutant in Complex with Fe(II), Alpha-Ketoglutarate and Hif-1 Alpha 35MER within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe350

b:46.4
occ:1.00
 O5 A:AKG1351 2.1 41.0 1.0
O2 A:AKG1351 2.2 52.3 1.0
NE2 A:HIS199 2.3 46.1 1.0
NE2 A:HIS279 2.3 44.6 1.0
O2 A:BCT3000 2.4 54.3 1.0
O1 A:BCT3000 2.6 53.2 1.0
C2 A:AKG1351 2.7 56.6 1.0
C1 A:AKG1351 2.8 38.5 1.0
C A:BCT3000 2.8 73.1 1.0
CD2 A:HIS279 3.1 40.7 1.0
CE1 A:HIS199 3.2 35.2 1.0
CD2 A:HIS199 3.3 32.8 1.0
CE1 A:HIS279 3.4 40.2 1.0
O1 A:AKG1351 4.0 83.7 1.0
CZ2 A:TRP296 4.1 53.3 1.0
O3 A:BCT3000 4.1 69.5 1.0
C3 A:AKG1351 4.1 35.8 1.0
O A:HOH1038 4.1 43.3 1.0
CG A:HIS279 4.3 47.1 1.0
ND1 A:HIS199 4.3 44.5 1.0
CG A:HIS199 4.4 37.1 1.0
ND1 A:HIS279 4.4 36.3 1.0
O A:HOH1141 4.6 85.5 1.0
ND2 A:ASN205 4.7 41.6 1.0
CH2 A:TRP296 4.8 93.1 1.0
C4 A:AKG1351 4.8 41.9 1.0

Reference:

K.S.Hewitson, S.L.Holmes, D.Ehrismann, A.P.Hardy, R.Chowdhury, C.J.Schofield, M.A.Mcdonough. Evidence That Two Enzyme-Derived Histidine Ligands Are Sufficient For Iron Binding and Catalysis By Factor Inhibiting Hif (Fih). J.Biol.Chem. V. 283 25971 2008.
ISSN: ISSN 0021-9258
PubMed: 18611856
DOI: 10.1074/JBC.M804999200
Page generated: Sun Dec 13 14:47:03 2020

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