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Iron in PDB 1s56: Crystal Structure of "Truncated" Hemoglobin N (Hbn) From Mycobacterium Tuberculosis, Soaked with Xe Atoms

Protein crystallography data

The structure of Crystal Structure of "Truncated" Hemoglobin N (Hbn) From Mycobacterium Tuberculosis, Soaked with Xe Atoms, PDB code: 1s56 was solved by M.Milani, A.Pesce, Y.Ouellet, S.Dewilde, J.Friedman, P.Ascenzi, M.Guertin, M.Bolognesi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.43
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.321, 61.959, 90.747, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 27.7

Other elements in 1s56:

The structure of Crystal Structure of "Truncated" Hemoglobin N (Hbn) From Mycobacterium Tuberculosis, Soaked with Xe Atoms also contains other interesting chemical elements:

Potassium (K) 1 atom
Xenon (Xe) 8 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of "Truncated" Hemoglobin N (Hbn) From Mycobacterium Tuberculosis, Soaked with Xe Atoms (pdb code 1s56). 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 "Truncated" Hemoglobin N (Hbn) From Mycobacterium Tuberculosis, Soaked with Xe Atoms, PDB code: 1s56:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1s56

Go back to Iron Binding Sites List in 1s56
Iron binding site 1 out of 2 in the Crystal Structure of "Truncated" Hemoglobin N (Hbn) From Mycobacterium Tuberculosis, Soaked with Xe Atoms


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 "Truncated" Hemoglobin N (Hbn) From Mycobacterium Tuberculosis, Soaked with Xe Atoms within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe144

b:28.2
occ:1.00
FE A:HEC144 0.0 28.2 1.0
NC A:HEC144 2.0 26.6 1.0
NB A:HEC144 2.0 27.5 1.0
NA A:HEC144 2.1 27.7 1.0
NE2 A:HIS81 2.1 26.8 1.0
ND A:HEC144 2.1 28.8 1.0
C1C A:HEC144 3.0 26.4 1.0
N A:CYN145 3.0 28.5 1.0
C4C A:HEC144 3.0 26.6 1.0
C4B A:HEC144 3.0 27.5 1.0
C1B A:HEC144 3.0 28.2 1.0
CE1 A:HIS81 3.1 28.0 1.0
C1D A:HEC144 3.1 28.5 1.0
C4A A:HEC144 3.1 27.9 1.0
C A:CYN145 3.1 28.8 1.0
C1A A:HEC144 3.1 27.0 1.0
C4D A:HEC144 3.2 28.4 1.0
CD2 A:HIS81 3.2 27.7 1.0
CHC A:HEC144 3.4 26.6 1.0
CHD A:HEC144 3.4 26.6 1.0
CHB A:HEC144 3.4 28.1 1.0
CHA A:HEC144 3.5 27.4 1.0
C2C A:HEC144 4.2 25.1 1.0
C3C A:HEC144 4.2 25.0 1.0
ND1 A:HIS81 4.2 26.7 1.0
C3B A:HEC144 4.2 27.3 1.0
C2B A:HEC144 4.2 27.9 1.0
CG A:HIS81 4.3 28.3 1.0
C3A A:HEC144 4.3 27.3 1.0
C2D A:HEC144 4.3 29.3 1.0
C2A A:HEC144 4.3 26.3 1.0
C3D A:HEC144 4.4 30.0 1.0
NE2 A:GLN58 4.8 20.7 1.0

Iron binding site 2 out of 2 in 1s56

Go back to Iron Binding Sites List in 1s56
Iron binding site 2 out of 2 in the Crystal Structure of "Truncated" Hemoglobin N (Hbn) From Mycobacterium Tuberculosis, Soaked with Xe Atoms


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 "Truncated" Hemoglobin N (Hbn) From Mycobacterium Tuberculosis, Soaked with Xe Atoms within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe144

b:27.1
occ:1.00
FE B:HEM144 0.0 27.1 1.0
NA B:HEM144 2.0 29.7 1.0
NE2 B:HIS81 2.0 24.5 1.0
NB B:HEM144 2.1 30.2 1.0
NC B:HEM144 2.1 29.5 1.0
ND B:HEM144 2.1 29.3 1.0
C B:CYN245 2.3 19.6 1.0
N B:CYN245 2.8 19.1 1.0
CE1 B:HIS81 2.9 24.7 1.0
C4A B:HEM144 2.9 30.0 1.0
C1B B:HEM144 3.0 31.6 1.0
C1D B:HEM144 3.0 28.5 1.0
C4C B:HEM144 3.0 28.8 1.0
C1A B:HEM144 3.1 30.2 1.0
CD2 B:HIS81 3.1 24.0 1.0
C4D B:HEM144 3.2 30.0 1.0
C4B B:HEM144 3.2 30.8 1.0
C1C B:HEM144 3.2 29.4 1.0
CHB B:HEM144 3.3 30.3 1.0
CHD B:HEM144 3.3 28.9 1.0
CHA B:HEM144 3.6 30.2 1.0
CHC B:HEM144 3.6 30.4 1.0
ND1 B:HIS81 4.0 23.9 1.0
C3A B:HEM144 4.2 29.7 1.0
CG B:HIS81 4.2 24.7 1.0
C2B B:HEM144 4.3 32.5 1.0
C2A B:HEM144 4.3 29.3 1.0
C3C B:HEM144 4.3 29.4 1.0
C2D B:HEM144 4.3 29.5 1.0
C3B B:HEM144 4.3 32.5 1.0
C2C B:HEM144 4.4 29.3 1.0
C3D B:HEM144 4.4 30.3 1.0
OE1 B:GLN58 4.6 33.7 1.0

Reference:

M.Milani, A.Pesce, Y.Ouellet, S.Dewilde, J.Friedman, P.Ascenzi, M.Guertin, M.Bolognesi. Heme-Ligand Tunneling in Group I Truncated Hemoglobins J.Biol.Chem. V. 279 21520 2004.
ISSN: ISSN 0021-9258
PubMed: 15016811
DOI: 10.1074/JBC.M401320200
Page generated: Sun Dec 13 14:31:09 2020

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