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Iron in PDB 4ni0: Quaternary R3 Co-Liganded Hemoglobin Structure in Complex with A Thiol Containing Compound

Protein crystallography data

The structure of Quaternary R3 Co-Liganded Hemoglobin Structure in Complex with A Thiol Containing Compound, PDB code: 4ni0 was solved by M.K.Safo, J.Meadows, T.-P.Ko, A.Nakagawa, W.Zapol, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.59 / 2.15
Space group P 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 62.064, 62.064, 173.882, 90.00, 90.00, 90.00
R / Rfree (%) 22.8 / 25.9

Iron Binding Sites:

The binding sites of Iron atom in the Quaternary R3 Co-Liganded Hemoglobin Structure in Complex with A Thiol Containing Compound (pdb code 4ni0). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Quaternary R3 Co-Liganded Hemoglobin Structure in Complex with A Thiol Containing Compound, PDB code: 4ni0:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 4ni0

Go back to Iron Binding Sites List in 4ni0
Iron binding site 1 out of 2 in the Quaternary R3 Co-Liganded Hemoglobin Structure in Complex with A Thiol Containing Compound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Quaternary R3 Co-Liganded Hemoglobin Structure in Complex with A Thiol Containing Compound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe202

b:35.1
occ:1.00
FE A:HEM202 0.0 35.1 1.0
C A:CMO201 1.8 24.2 1.0
NE2 A:HIS87 2.0 29.8 1.0
NA A:HEM202 2.0 43.8 1.0
NB A:HEM202 2.0 37.1 1.0
ND A:HEM202 2.0 50.2 1.0
NC A:HEM202 2.1 42.9 1.0
CD2 A:HIS87 2.9 26.0 1.0
C1B A:HEM202 3.0 43.5 1.0
C4A A:HEM202 3.0 38.8 1.0
O A:CMO201 3.0 44.4 1.0
CE1 A:HIS87 3.0 33.0 1.0
C4D A:HEM202 3.0 43.1 1.0
C1A A:HEM202 3.0 37.6 1.0
C4B A:HEM202 3.1 37.0 1.0
C1D A:HEM202 3.1 50.5 1.0
C1C A:HEM202 3.1 37.0 1.0
C4C A:HEM202 3.1 49.3 1.0
CHB A:HEM202 3.4 46.0 1.0
CHA A:HEM202 3.4 32.1 1.0
CHC A:HEM202 3.5 38.6 1.0
CHD A:HEM202 3.5 53.4 1.0
CG A:HIS87 4.1 41.6 1.0
ND1 A:HIS87 4.1 31.1 1.0
C3A A:HEM202 4.2 43.6 1.0
NE2 A:HIS58 4.2 39.3 1.0
C2B A:HEM202 4.3 39.4 1.0
C2A A:HEM202 4.3 46.6 1.0
C3D A:HEM202 4.3 45.7 1.0
C3B A:HEM202 4.3 41.8 1.0
C2D A:HEM202 4.4 48.2 1.0
C2C A:HEM202 4.4 51.0 1.0
C3C A:HEM202 4.4 50.4 1.0
CG2 A:VAL62 5.0 37.2 1.0

Iron binding site 2 out of 2 in 4ni0

Go back to Iron Binding Sites List in 4ni0
Iron binding site 2 out of 2 in the Quaternary R3 Co-Liganded Hemoglobin Structure in Complex with A Thiol Containing Compound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Quaternary R3 Co-Liganded Hemoglobin Structure in Complex with A Thiol Containing Compound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe202

b:45.7
occ:1.00
FE B:HEM202 0.0 45.7 1.0
C B:CMO201 1.9 48.4 1.0
NB B:HEM202 2.0 39.2 1.0
ND B:HEM202 2.0 42.5 1.0
NA B:HEM202 2.0 49.2 1.0
NC B:HEM202 2.0 45.1 1.0
NE2 B:HIS92 2.1 55.9 1.0
C4B B:HEM202 3.0 46.3 1.0
C4D B:HEM202 3.0 38.6 1.0
C1D B:HEM202 3.0 51.5 1.0
C1B B:HEM202 3.0 44.2 1.0
O B:CMO201 3.1 50.0 1.0
C4A B:HEM202 3.1 41.9 1.0
CD2 B:HIS92 3.1 56.5 1.0
C1C B:HEM202 3.1 40.2 1.0
C1A B:HEM202 3.1 43.2 1.0
CE1 B:HIS92 3.1 46.0 1.0
C4C B:HEM202 3.1 40.2 1.0
CHC B:HEM202 3.4 47.8 1.0
CHB B:HEM202 3.4 43.1 1.0
CHD B:HEM202 3.5 46.3 1.0
CHA B:HEM202 3.5 29.9 1.0
C3D B:HEM202 4.2 40.1 1.0
ND1 B:HIS92 4.2 53.3 1.0
CG B:HIS92 4.2 55.8 1.0
C2D B:HEM202 4.3 45.2 1.0
C3B B:HEM202 4.3 42.7 1.0
C2B B:HEM202 4.3 45.1 1.0
C2A B:HEM202 4.3 51.7 1.0
C3A B:HEM202 4.3 49.8 1.0
C3C B:HEM202 4.3 40.6 1.0
C2C B:HEM202 4.4 50.3 1.0
CE1 B:HIS63 4.5 60.7 1.0
CG2 B:VAL67 4.8 46.7 1.0

Reference:

A.Nakagawa, F.E.Lui, D.Wassaf, R.Yefidoff-Freedman, D.Casalena, M.A.Palmer, J.Meadows, A.Mozzarelli, L.Ronda, O.Abdulmalik, K.D.Bloch, M.K.Safo, W.M.Zapol. Identification of A Small Molecule That Increases Hemoglobin Oxygen Affinity and Reduces Ss Erythrocyte Sickling. Acs Chem.Biol. V. 9 2318 2014.
ISSN: ISSN 1554-8929
PubMed: 25061917
DOI: 10.1021/CB500230B
Page generated: Mon Aug 5 07:37:53 2024

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