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Iron in PDB 4z2w: Factor Inhibiting Hif in Complex with Fe, and Alpha-Ketoglutarate

Enzymatic activity of Factor Inhibiting Hif in Complex with Fe, and Alpha-Ketoglutarate

All present enzymatic activity of Factor Inhibiting Hif in Complex with Fe, and Alpha-Ketoglutarate:
1.14.11.30;

Protein crystallography data

The structure of Factor Inhibiting Hif in Complex with Fe, and Alpha-Ketoglutarate, PDB code: 4z2w was solved by C.Y.Taabazuing, S.C.Garman, M.J.Knapp, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 61.00 / 2.50
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 86.570, 86.570, 147.230, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 24.6

Iron Binding Sites:

The binding sites of Iron atom in the Factor Inhibiting Hif in Complex with Fe, and Alpha-Ketoglutarate (pdb code 4z2w). 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 in Complex with Fe, and Alpha-Ketoglutarate, PDB code: 4z2w:

Iron binding site 1 out of 1 in 4z2w

Go back to Iron Binding Sites List in 4z2w
Iron binding site 1 out of 1 in the Factor Inhibiting Hif in Complex with Fe, and Alpha-Ketoglutarate


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 in Complex with Fe, and Alpha-Ketoglutarate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe403

b:36.6
occ:1.00
NE2 A:HIS199 2.0 40.0 1.0
NE2 A:HIS279 2.0 38.0 1.0
O2 A:AKG401 2.0 40.2 1.0
O A:HOH510 2.0 46.0 1.0
OD2 A:ASP201 2.0 26.1 1.0
O5 A:AKG401 2.3 36.3 1.0
C1 A:AKG401 2.8 38.6 1.0
C2 A:AKG401 2.9 33.0 1.0
CE1 A:HIS199 2.9 40.0 1.0
CD2 A:HIS279 2.9 33.5 1.0
CD2 A:HIS199 3.0 35.4 1.0
CE1 A:HIS279 3.0 33.7 1.0
CG A:ASP201 3.0 28.9 1.0
OD1 A:ASP201 3.3 34.1 1.0
O1 A:AKG401 4.0 56.3 1.0
O A:HOH529 4.0 34.6 1.0
ND1 A:HIS199 4.0 35.5 1.0
CG A:HIS279 4.1 31.9 1.0
ND1 A:HIS279 4.1 32.9 1.0
CG A:HIS199 4.1 36.3 1.0
O2 A:PEG402 4.2 72.5 1.0
C3 A:AKG401 4.4 31.8 1.0
CB A:ASP201 4.4 29.1 1.0
CZ2 A:TRP296 4.6 59.9 1.0
C4 A:PEG402 4.8 71.3 1.0
C3 A:PEG402 4.9 70.4 1.0
O4 A:PEG402 4.9 76.2 1.0

Reference:

C.Y.Taabazuing, J.Fermann, S.Garman, M.J.Knapp. Substrate Promotes Productive Gas Binding in the Alpha-Ketoglutarate-Dependent Oxygenase Fih. Biochemistry V. 55 277 2016.
ISSN: ISSN 0006-2960
PubMed: 26727884
DOI: 10.1021/ACS.BIOCHEM.5B01003
Page generated: Mon Aug 5 17:06:30 2024

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