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Iron in PDB 1twr: Crystal Structures of Ferrous and Ferrous-No Forms of Verdoheme in A Complex with Human Heme Oxygenase-1: Catalytic Implications For Heme Cleavage

Enzymatic activity of Crystal Structures of Ferrous and Ferrous-No Forms of Verdoheme in A Complex with Human Heme Oxygenase-1: Catalytic Implications For Heme Cleavage

All present enzymatic activity of Crystal Structures of Ferrous and Ferrous-No Forms of Verdoheme in A Complex with Human Heme Oxygenase-1: Catalytic Implications For Heme Cleavage:
1.14.99.3;

Protein crystallography data

The structure of Crystal Structures of Ferrous and Ferrous-No Forms of Verdoheme in A Complex with Human Heme Oxygenase-1: Catalytic Implications For Heme Cleavage, PDB code: 1twr was solved by L.Lad, P.R.Ortiz De Montellano, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 61.038, 54.258, 70.249, 90.00, 98.12, 90.00
R / Rfree (%) 24.1 / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structures of Ferrous and Ferrous-No Forms of Verdoheme in A Complex with Human Heme Oxygenase-1: Catalytic Implications For Heme Cleavage (pdb code 1twr). 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 Structures of Ferrous and Ferrous-No Forms of Verdoheme in A Complex with Human Heme Oxygenase-1: Catalytic Implications For Heme Cleavage, PDB code: 1twr:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1twr

Go back to Iron Binding Sites List in 1twr
Iron binding site 1 out of 2 in the Crystal Structures of Ferrous and Ferrous-No Forms of Verdoheme in A Complex with Human Heme Oxygenase-1: Catalytic Implications For Heme Cleavage


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 Ferrous and Ferrous-No Forms of Verdoheme in A Complex with Human Heme Oxygenase-1: Catalytic Implications For Heme Cleavage within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:51.4
occ:1.00
 FE A:VER300 0.0 51.4 1.0
N A:NO400 2.0 50.9 0.8
NB A:VER300 2.0 52.9 1.0
NC A:VER300 2.0 52.8 1.0
NA A:VER300 2.0 51.1 1.0
ND A:VER300 2.0 52.8 1.0
NE2 A:HIS25 2.4 56.2 1.0
CE1 A:HIS25 2.9 56.3 1.0
O A:NO400 3.0 52.5 0.8
C4B A:VER300 3.0 53.1 1.0
C1C A:VER300 3.1 52.9 1.0
C4C A:VER300 3.1 52.8 1.0
C1D A:VER300 3.1 52.5 1.0
C1A A:VER300 3.1 53.0 1.0
C4D A:VER300 3.1 52.7 1.0
C1B A:VER300 3.1 53.1 1.0
C4A A:VER300 3.1 53.1 1.0
O A:VER300 3.4 53.1 1.0
CHD A:VER300 3.5 52.6 1.0
CHA A:VER300 3.5 52.9 1.0
CHB A:VER300 3.5 53.2 1.0
CD2 A:HIS25 3.6 56.1 1.0
ND1 A:HIS25 4.1 56.5 1.0
C3B A:VER300 4.3 52.3 1.0
C2C A:VER300 4.3 51.9 1.0
C2D A:VER300 4.3 51.5 1.0
C3C A:VER300 4.3 53.0 1.0
C3D A:VER300 4.3 51.6 1.0
CMA A:VER300 4.3 53.0 0.0
C3A A:VER300 4.3 53.2 1.0
C2B A:VER300 4.4 53.2 1.0
CG A:HIS25 4.5 56.1 1.0
O A:HOH439 4.5 64.5 1.0
O A:GLY139 4.9 48.1 1.0
CA A:GLY139 5.0 47.1 1.0

Iron binding site 2 out of 2 in 1twr

Go back to Iron Binding Sites List in 1twr
Iron binding site 2 out of 2 in the Crystal Structures of Ferrous and Ferrous-No Forms of Verdoheme in A Complex with Human Heme Oxygenase-1: Catalytic Implications For Heme Cleavage


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structures of Ferrous and Ferrous-No Forms of Verdoheme in A Complex with Human Heme Oxygenase-1: Catalytic Implications For Heme Cleavage within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe300

b:61.4
occ:1.00
 FE B:VER300 0.0 61.4 1.0
N B:NO401 1.8 61.1 0.8
NA B:VER300 2.0 61.7 1.0
NC B:VER300 2.0 61.6 1.0
ND B:VER300 2.0 61.5 1.0
NB B:VER300 2.0 61.6 1.0
NE2 B:HIS25 2.5 67.0 1.0
CE1 B:HIS25 2.9 67.0 1.0
O B:NO401 2.9 61.1 0.8
C4B B:VER300 3.1 61.8 1.0
C1A B:VER300 3.1 61.6 1.0
C1C B:VER300 3.1 61.7 1.0
C4C B:VER300 3.1 61.8 1.0
C4D B:VER300 3.1 61.3 1.0
C1D B:VER300 3.1 61.2 1.0
C4A B:VER300 3.1 61.6 1.0
C1B B:VER300 3.1 61.7 1.0
CHA B:VER300 3.4 61.6 0.3
O B:VER300 3.4 62.0 1.0
CHD B:VER300 3.5 61.5 1.0
CHB B:VER300 3.5 61.8 1.0
CD2 B:HIS25 3.8 66.9 1.0
ND1 B:HIS25 4.1 67.1 1.0
C3B B:VER300 4.3 61.8 0.3
C2C B:VER300 4.3 61.8 1.0
CMA B:VER300 4.3 61.6 0.3
C2D B:VER300 4.3 61.1 1.0
C3D B:VER300 4.3 61.1 1.0
C3A B:VER300 4.3 61.7 0.3
C3C B:VER300 4.3 61.9 1.0
C2B B:VER300 4.4 61.8 0.3
OE2 B:GLU29 4.6 70.3 1.0
CG B:HIS25 4.6 66.9 1.0
O B:GLY139 5.0 43.1 1.0

Reference:

L.Lad, P.R.Ortiz De Montellano, T.L.Poulos. Crystal Structures of Ferrous and Ferrous-No Forms of Verdoheme in A Complex with Human Heme Oxygenase-1: Catalytic Implications For Heme Cleavage. J.Inorg.Biochem. V. 98 1686 2004.
ISSN: ISSN 0162-0134
PubMed: 15522396
DOI: 10.1016/J.JINORGBIO.2004.07.004
Page generated: Sat Aug 3 15:21:21 2024

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