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Iron in PDB 1twn: 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: 1twn 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) 50.00 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 61.607, 54.562, 71.720, 90.00, 99.24, 90.00
R / Rfree (%) 23.8 / 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 1twn). 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: 1twn:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1twn

Go back to Iron Binding Sites List in 1twn
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:36.0
occ:1.00
 FE A:VER300 0.0 36.0 1.0
NB A:VER300 2.0 36.5 1.0
NC A:VER300 2.0 35.2 1.0
NA A:VER300 2.0 37.2 1.0
ND A:VER300 2.0 35.6 1.0
NE2 A:HIS25 2.1 35.4 1.0
C1B A:VER300 3.0 37.0 1.0
C4B A:VER300 3.0 36.1 1.0
CE1 A:HIS25 3.0 35.0 1.0
C4C A:VER300 3.0 35.2 1.0
C4A A:VER300 3.0 37.5 1.0
C1C A:VER300 3.1 35.5 1.0
C1D A:VER300 3.1 35.1 1.0
C1A A:VER300 3.1 37.0 1.0
C4D A:VER300 3.1 36.2 1.0
CD2 A:HIS25 3.2 34.7 1.0
O A:VER300 3.4 35.5 1.0
CHB A:VER300 3.4 37.1 1.0
CHD A:VER300 3.4 34.4 1.0
CHA A:VER300 3.5 36.7 1.0
ND1 A:HIS25 4.2 35.6 1.0
C3A A:VER300 4.3 37.6 1.0
C2B A:VER300 4.3 37.1 1.0
C3B A:VER300 4.3 37.2 1.0
CG A:HIS25 4.3 35.1 1.0
C3C A:VER300 4.3 35.4 1.0
C2C A:VER300 4.3 35.6 1.0
C2D A:VER300 4.3 35.5 1.0
C3D A:VER300 4.3 36.2 1.0
N A:GLY143 4.4 44.1 1.0
CA A:GLY143 4.5 45.2 1.0
O A:GLY139 4.6 33.8 1.0
CA A:GLY139 4.7 32.5 1.0

Iron binding site 2 out of 2 in 1twn

Go back to Iron Binding Sites List in 1twn
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:55.9
occ:1.00
 FE B:VER300 0.0 55.9 1.0
NA B:VER300 2.0 56.5 1.0
NB B:VER300 2.0 56.5 1.0
ND B:VER300 2.0 55.5 1.0
NC B:VER300 2.0 55.5 1.0
NE2 B:HIS25 2.1 54.0 1.0
CE1 B:HIS25 2.9 52.4 1.0
C1A B:VER300 3.1 56.5 1.0
C1D B:VER300 3.1 55.7 1.0
C1B B:VER300 3.1 57.0 1.0
C4A B:VER300 3.1 57.2 1.0
C4B B:VER300 3.1 56.7 1.0
C4D B:VER300 3.1 55.9 1.0
C1C B:VER300 3.1 55.6 1.0
C4C B:VER300 3.1 55.6 1.0
CD2 B:HIS25 3.3 51.6 1.0
CHD B:VER300 3.5 55.4 1.0
CHB B:VER300 3.5 57.0 1.0
CHA B:VER300 3.5 55.8 1.0
O B:VER300 3.5 55.9 1.0
ND1 B:HIS25 4.1 52.0 1.0
CG B:HIS25 4.3 51.0 1.0
C3A B:VER300 4.3 57.5 1.0
C2B B:VER300 4.3 57.5 1.0
C2D B:VER300 4.3 55.6 1.0
C3D B:VER300 4.3 56.2 1.0
C2C B:VER300 4.3 55.7 1.0
C3B B:VER300 4.3 57.3 1.0
C3C B:VER300 4.3 55.8 1.0
O B:GLY139 4.8 29.6 1.0
CA B:GLY139 5.0 28.7 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: Sun Dec 13 14:32:55 2020

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