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Iron in PDB 2g6m: Structure of Rat Nnos Heme Domain (BH4 Bound) Complexed with Co

Enzymatic activity of Structure of Rat Nnos Heme Domain (BH4 Bound) Complexed with Co

All present enzymatic activity of Structure of Rat Nnos Heme Domain (BH4 Bound) Complexed with Co:
1.14.13.39;

Protein crystallography data

The structure of Structure of Rat Nnos Heme Domain (BH4 Bound) Complexed with Co, PDB code: 2g6m was solved by H.Li, J.Igarashi, J.Jamal, W.Yang, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.98 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.850, 110.970, 164.370, 90.00, 90.00, 90.00
R / Rfree (%) 22 / 25.1

Other elements in 2g6m:

The structure of Structure of Rat Nnos Heme Domain (BH4 Bound) Complexed with Co also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Rat Nnos Heme Domain (BH4 Bound) Complexed with Co (pdb code 2g6m). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Rat Nnos Heme Domain (BH4 Bound) Complexed with Co, PDB code: 2g6m:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 2g6m

Go back to Iron Binding Sites List in 2g6m
Iron binding site 1 out of 2 in the Structure of Rat Nnos Heme Domain (BH4 Bound) Complexed with Co


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Rat Nnos Heme Domain (BH4 Bound) Complexed with Co within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe750

b:24.2
occ:1.00
FE A:HEM750 0.0 24.2 1.0
C A:CMO920 1.7 33.0 1.0
NC A:HEM750 2.0 22.5 1.0
NA A:HEM750 2.0 24.6 1.0
ND A:HEM750 2.1 24.7 1.0
NB A:HEM750 2.1 23.0 1.0
SG A:CYS415 2.4 23.2 1.0
O A:CMO920 2.9 29.8 1.0
C1C A:HEM750 3.1 24.8 1.0
C4A A:HEM750 3.1 23.6 1.0
C4C A:HEM750 3.1 22.5 1.0
C1B A:HEM750 3.1 23.6 1.0
C4B A:HEM750 3.1 23.8 1.0
C1A A:HEM750 3.1 22.9 1.0
C4D A:HEM750 3.1 23.3 1.0
C1D A:HEM750 3.1 24.2 1.0
CB A:CYS415 3.4 22.6 1.0
CHC A:HEM750 3.4 25.0 1.0
CHB A:HEM750 3.4 22.5 1.0
CHD A:HEM750 3.4 23.0 1.0
CHA A:HEM750 3.5 22.8 1.0
CA A:CYS415 4.2 20.1 1.0
C3C A:HEM750 4.3 25.3 1.0
C2C A:HEM750 4.3 24.9 1.0
C3A A:HEM750 4.3 23.8 1.0
C2A A:HEM750 4.3 23.0 1.0
C2B A:HEM750 4.4 24.1 1.0
C3D A:HEM750 4.4 23.8 1.0
C2D A:HEM750 4.4 23.7 1.0
C3B A:HEM750 4.4 26.9 1.0
NH1 A:ARG770 4.4 25.8 1.0
NE1 A:TRP409 4.5 24.6 1.0
CZ A:ARG770 4.7 25.1 1.0
C A:CYS415 4.9 21.5 1.0
N A:GLY417 5.0 20.8 1.0

Iron binding site 2 out of 2 in 2g6m

Go back to Iron Binding Sites List in 2g6m
Iron binding site 2 out of 2 in the Structure of Rat Nnos Heme Domain (BH4 Bound) Complexed with Co


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Rat Nnos Heme Domain (BH4 Bound) Complexed with Co within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe750

b:23.5
occ:1.00
FE B:HEM750 0.0 23.5 1.0
C B:CMO920 1.7 29.9 1.0
NB B:HEM750 2.0 23.0 1.0
NA B:HEM750 2.0 22.7 1.0
NC B:HEM750 2.1 21.3 1.0
ND B:HEM750 2.1 22.2 1.0
SG B:CYS415 2.4 22.7 1.0
O B:CMO920 2.8 31.3 1.0
C4B B:HEM750 3.0 23.4 1.0
C1B B:HEM750 3.0 25.3 1.0
C1A B:HEM750 3.1 20.0 1.0
C4A B:HEM750 3.1 22.5 1.0
C1C B:HEM750 3.1 22.0 1.0
C4C B:HEM750 3.1 22.1 1.0
C1D B:HEM750 3.1 23.7 1.0
C4D B:HEM750 3.1 20.7 1.0
CB B:CYS415 3.4 19.8 1.0
CHC B:HEM750 3.4 17.8 1.0
CHB B:HEM750 3.4 23.4 1.0
CHA B:HEM750 3.4 19.3 1.0
CHD B:HEM750 3.5 22.8 1.0
CA B:CYS415 4.1 20.1 1.0
C3B B:HEM750 4.3 25.0 1.0
C2B B:HEM750 4.3 23.9 1.0
C2A B:HEM750 4.3 21.5 1.0
C3A B:HEM750 4.3 21.0 1.0
C3C B:HEM750 4.3 22.6 1.0
C2D B:HEM750 4.3 22.4 1.0
C2C B:HEM750 4.4 20.9 1.0
C3D B:HEM750 4.4 23.4 1.0
NH1 B:ARG771 4.4 24.9 1.0
NE1 B:TRP409 4.5 22.2 1.0
CZ B:ARG771 4.7 24.0 1.0
N B:GLY417 4.9 20.2 1.0
C B:CYS415 4.9 22.0 1.0
NH2 B:ARG771 4.9 22.5 1.0

Reference:

H.Li, J.Igarashi, J.Jamal, W.Yang, T.L.Poulos. Structural Studies of Constitutive Nitric Oxide Synthases with Diatomic Ligands Bound. J.Biol.Inorg.Chem. V. 11 753 2006.
ISSN: ISSN 0949-8257
PubMed: 16804678
DOI: 10.1007/S00775-006-0123-8
Page generated: Thu Jul 17 01:31:00 2025

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