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Iron in PDB 1ey2: Human Homogentisate Dioxygenase with Fe(II)

Enzymatic activity of Human Homogentisate Dioxygenase with Fe(II)

All present enzymatic activity of Human Homogentisate Dioxygenase with Fe(II):
1.13.11.5;

Protein crystallography data

The structure of Human Homogentisate Dioxygenase with Fe(II), PDB code: 1ey2 was solved by D.E.Timm, G.P.Titus, M.A.Penalva, H.A.Mueller, S.M.De Cordoba, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.30
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 157.809, 157.809, 95.147, 90.00, 90.00, 120.00
R / Rfree (%) 19.3 / 24.2

Iron Binding Sites:

The binding sites of Iron atom in the Human Homogentisate Dioxygenase with Fe(II) (pdb code 1ey2). 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 Human Homogentisate Dioxygenase with Fe(II), PDB code: 1ey2:

Iron binding site 1 out of 1 in 1ey2

Go back to Iron Binding Sites List in 1ey2
Iron binding site 1 out of 1 in the Human Homogentisate Dioxygenase with Fe(II)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Homogentisate Dioxygenase with Fe(II) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1001

b:39.6
occ:1.00
O A:HOH2232 1.9 46.9 1.0
NE2 A:HIS371 2.3 29.9 1.0
ND1 A:HIS335 2.4 28.6 1.0
OE2 A:GLU341 2.4 37.8 1.0
O A:HOH2231 2.6 49.6 1.0
OE1 A:GLU341 2.7 35.5 1.0
CD A:GLU341 2.9 32.7 1.0
CD2 A:HIS371 3.1 30.3 1.0
CE1 A:HIS335 3.1 30.1 1.0
CE1 A:HIS371 3.4 31.9 1.0
CG A:HIS335 3.5 30.1 1.0
O A:HOH2127 3.7 38.7 1.0
CB A:HIS335 3.9 25.9 1.0
CG A:GLU341 4.3 27.9 1.0
CG A:HIS371 4.4 29.0 1.0
NE2 A:HIS335 4.4 28.8 1.0
ND1 A:HIS371 4.5 30.9 1.0
CD2 A:HIS335 4.6 29.7 1.0
ND2 A:ASN337 4.6 29.0 1.0
CB A:ASN337 4.9 25.0 1.0

Reference:

G.P.Titus, H.A.Mueller, J.Burgner, S.Rodriguez De Cordoba, M.A.Penalva, D.E.Timm. Crystal Structure of Human Homogentisate Dioxygenase. Nat.Struct.Biol. V. 7 542 2000.
ISSN: ISSN 1072-8368
PubMed: 10876237
DOI: 10.1038/76756
Page generated: Sun Dec 13 14:13:00 2020

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