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Iron in PDB 2huo: Crystal Structure of Mouse Myo-Inositol Oxygenase in Complex with Substrate

Enzymatic activity of Crystal Structure of Mouse Myo-Inositol Oxygenase in Complex with Substrate

All present enzymatic activity of Crystal Structure of Mouse Myo-Inositol Oxygenase in Complex with Substrate:
1.13.99.1;

Protein crystallography data

The structure of Crystal Structure of Mouse Myo-Inositol Oxygenase in Complex with Substrate, PDB code: 2huo was solved by P.M.Brown, T.T.Caradoc-Davies, J.M.J.Dickson, G.J.S.Cooper, K.M.Loomes, E.N.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 57.26 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.602, 77.202, 85.397, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 25.6

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Mouse Myo-Inositol Oxygenase in Complex with Substrate (pdb code 2huo). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Mouse Myo-Inositol Oxygenase in Complex with Substrate, PDB code: 2huo:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 2huo

Go back to Iron Binding Sites List in 2huo
Iron binding site 1 out of 2 in the Crystal Structure of Mouse Myo-Inositol Oxygenase in Complex with Substrate


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 Mouse Myo-Inositol Oxygenase in Complex with Substrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe301

b:26.2
occ:1.00
O A:OH304 2.0 29.1 1.0
NE2 A:HIS123 2.0 29.4 1.0
NE2 A:HIS98 2.0 25.0 1.0
OD2 A:ASP124 2.0 29.1 1.0
OD1 A:ASP253 2.1 33.0 1.0
O A:HOH306 2.1 15.3 1.0
CD2 A:HIS123 2.9 24.7 1.0
CE1 A:HIS98 2.9 27.3 1.0
CG A:ASP124 3.0 30.4 1.0
CG A:ASP253 3.1 33.0 1.0
CE1 A:HIS123 3.1 28.2 1.0
CD2 A:HIS98 3.2 25.8 1.0
OD2 A:ASP253 3.4 30.7 1.0
OD1 A:ASP124 3.4 27.4 1.0
FE A:FE302 3.6 21.1 1.0
O1 A:INS303 3.7 8.8 1.0
ND1 A:HIS98 4.1 25.6 1.0
CG A:HIS123 4.1 31.5 1.0
ND1 A:HIS123 4.1 28.9 1.0
CG A:HIS98 4.2 26.5 1.0
CB A:ASP124 4.2 29.8 1.0
C1 A:INS303 4.3 18.7 1.0
O A:HOH358 4.4 30.0 1.0
CB A:ASP253 4.4 32.8 1.0
CE A:LYS257 4.8 30.7 1.0
CD2 A:HIS220 4.8 16.4 1.0
O A:ASP253 4.8 33.6 1.0
NE2 A:HIS220 4.8 7.4 1.0
OG1 A:THR102 4.9 28.4 1.0
CA A:ASP253 4.9 32.9 1.0
NZ A:LYS257 4.9 31.6 1.0
O6 A:INS303 4.9 22.9 1.0
NZ A:LYS127 4.9 13.2 1.0

Iron binding site 2 out of 2 in 2huo

Go back to Iron Binding Sites List in 2huo
Iron binding site 2 out of 2 in the Crystal Structure of Mouse Myo-Inositol Oxygenase in Complex with Substrate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Mouse Myo-Inositol Oxygenase in Complex with Substrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe302

b:21.1
occ:1.00
NE2 A:HIS194 2.0 24.0 1.0
O A:OH304 2.0 29.1 1.0
OD1 A:ASP124 2.1 27.4 1.0
NE2 A:HIS220 2.1 7.4 1.0
O6 A:INS303 2.1 22.9 1.0
O1 A:INS303 2.1 8.8 1.0
CD2 A:HIS220 2.8 16.4 1.0
C1 A:INS303 2.9 18.7 1.0
C6 A:INS303 2.9 19.1 1.0
CE1 A:HIS194 3.0 22.8 1.0
CD2 A:HIS194 3.0 26.6 1.0
CG A:ASP124 3.0 30.4 1.0
CE1 A:HIS220 3.3 29.5 1.0
OD2 A:ASP124 3.3 29.1 1.0
FE A:FE301 3.6 26.2 1.0
CD2 A:HIS123 4.0 24.7 1.0
OG A:SER221 4.0 29.6 1.0
ND1 A:HIS194 4.1 26.5 1.0
CG A:HIS220 4.1 18.8 1.0
O A:HOH306 4.1 15.3 1.0
CG A:HIS194 4.1 25.7 1.0
C5 A:INS303 4.2 21.7 1.0
ND1 A:HIS220 4.3 12.0 1.0
C2 A:INS303 4.3 13.5 1.0
OD2 A:ASP253 4.4 30.7 1.0
CB A:ASP124 4.4 29.8 1.0
NZ A:LYS127 4.4 13.2 1.0
NE2 A:HIS123 4.4 29.4 1.0
OD1 A:ASP195 4.6 33.8 1.0
O A:HOH358 4.7 30.0 1.0
CE A:LYS127 4.8 11.6 1.0
CA A:ASP124 4.8 31.1 1.0
O2 A:INS303 4.9 9.4 1.0
O5 A:INS303 4.9 25.5 1.0
OD1 A:ASP253 4.9 33.0 1.0

Reference:

P.M.Brown, T.T.Caradoc-Davies, J.M.Dickson, G.J.Cooper, K.M.Loomes, E.N.Baker. Crystal Structure of A Substrate Complex of Myo-Inositol Oxygenase, A Di-Iron Oxygenase with A Key Role in Inositol Metabolism. Proc.Natl.Acad.Sci.Usa V. 103 15032 2006.
ISSN: ISSN 0027-8424
PubMed: 17012379
DOI: 10.1073/PNAS.0605143103
Page generated: Thu Jul 17 02:09:04 2025

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