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Iron in PDB 1p3v: Crystal Structures of the No-and Co-Bound Heme Oxygenase From Neisseria Meningitidis: Implications For Oxygen Activation

Enzymatic activity of Crystal Structures of the No-and Co-Bound Heme Oxygenase From Neisseria Meningitidis: Implications For Oxygen Activation

All present enzymatic activity of Crystal Structures of the No-and Co-Bound Heme Oxygenase From Neisseria Meningitidis: Implications For Oxygen Activation:
1.14.99.3;

Protein crystallography data

The structure of Crystal Structures of the No-and Co-Bound Heme Oxygenase From Neisseria Meningitidis: Implications For Oxygen Activation, PDB code: 1p3v was solved by J.Friedman, L.Lad, R.Deshmukh, H.Li, A.Wilks, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.25
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 60.449, 60.449, 102.361, 90.00, 90.00, 90.00
R / Rfree (%) 24.9 / 28.6

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structures of the No-and Co-Bound Heme Oxygenase From Neisseria Meningitidis: Implications For Oxygen Activation (pdb code 1p3v). 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 Crystal Structures of the No-and Co-Bound Heme Oxygenase From Neisseria Meningitidis: Implications For Oxygen Activation, PDB code: 1p3v:

Iron binding site 1 out of 1 in 1p3v

Go back to Iron Binding Sites List in 1p3v
Iron binding site 1 out of 1 in the Crystal Structures of the No-and Co-Bound Heme Oxygenase From Neisseria Meningitidis: Implications For Oxygen Activation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structures of the No-and Co-Bound Heme Oxygenase From Neisseria Meningitidis: Implications For Oxygen Activation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:41.9
occ:1.00
 FE A:HEM300 0.0 41.9 1.0
ND A:HEM300 2.0 42.0 1.0
C A:CMO400 2.0 42.0 0.5
NA A:HEM300 2.0 42.3 1.0
NB A:HEM300 2.0 42.1 1.0
NC A:HEM300 2.0 41.9 1.0
NE2 A:HIS23 2.2 41.1 1.0
C4D A:HEM300 3.0 42.4 1.0
C1A A:HEM300 3.0 42.7 1.0
C1D A:HEM300 3.0 42.2 1.0
CE1 A:HIS23 3.0 40.7 1.0
C1C A:HEM300 3.1 42.1 1.0
C4A A:HEM300 3.1 42.6 1.0
C1B A:HEM300 3.1 42.4 1.0
C4C A:HEM300 3.1 42.0 1.0
C4B A:HEM300 3.1 42.2 1.0
O A:CMO400 3.1 42.0 0.5
CD2 A:HIS23 3.2 40.5 1.0
CHA A:HEM300 3.4 42.6 1.0
CHD A:HEM300 3.5 41.9 1.0
CHC A:HEM300 3.5 42.3 1.0
CHB A:HEM300 3.5 42.4 1.0
C3D A:HEM300 4.2 42.4 1.0
ND1 A:HIS23 4.2 40.4 1.0
C2D A:HEM300 4.2 42.3 1.0
C2A A:HEM300 4.3 43.1 1.0
C2C A:HEM300 4.3 42.0 1.0
C3A A:HEM300 4.3 42.9 1.0
C2B A:HEM300 4.3 42.3 1.0
CG A:HIS23 4.3 40.3 1.0
C3C A:HEM300 4.3 41.9 1.0
C3B A:HEM300 4.3 42.4 1.0
CA A:SER117 4.7 46.0 1.0
CA A:GLY120 4.8 54.5 1.0

Reference:

J.Friedman, L.Lad, R.Deshmukh, H.Li, A.Wilks, T.L.Poulos. Crystal Structures of the No- and Co-Bound Heme Oxygenase From Neisseriae Meningitidis. Implications For O2 Activation J.Biol.Chem. V. 278 34654 2003.
ISSN: ISSN 0021-9258
PubMed: 12819228
DOI: 10.1074/JBC.M302985200
Page generated: Sat Aug 3 12:57:33 2024

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