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Iron in PDB 5kke: Crystal Structure of A Domain-Swapped Dimer of Yeast Iso-1-Cytochrome C with CYMAL5

Protein crystallography data

The structure of Crystal Structure of A Domain-Swapped Dimer of Yeast Iso-1-Cytochrome C with CYMAL5, PDB code: 5kke was solved by B.E.Bowler, F.G.Whitby, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.98 / 1.70
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 49.740, 69.326, 72.482, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / 20.4

Other elements in 5kke:

The structure of Crystal Structure of A Domain-Swapped Dimer of Yeast Iso-1-Cytochrome C with CYMAL5 also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of A Domain-Swapped Dimer of Yeast Iso-1-Cytochrome C with CYMAL5 (pdb code 5kke). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of A Domain-Swapped Dimer of Yeast Iso-1-Cytochrome C with CYMAL5, PDB code: 5kke:

Iron binding site 1 out of 1 in 5kke

Go back to Iron Binding Sites List in 5kke
Iron binding site 1 out of 1 in the Crystal Structure of A Domain-Swapped Dimer of Yeast Iso-1-Cytochrome C with CYMAL5


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 A Domain-Swapped Dimer of Yeast Iso-1-Cytochrome C with CYMAL5 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:23.3
occ:1.00
FE A:HEM201 0.0 23.3 1.0
NC A:HEM201 2.0 22.1 1.0
ND A:HEM201 2.0 19.3 1.0
NA A:HEM201 2.0 23.0 1.0
NB A:HEM201 2.0 19.1 1.0
O A:HOH347 2.1 26.3 1.0
NE2 A:HIS18 2.1 23.1 1.0
C1D A:HEM201 3.0 21.2 1.0
C4B A:HEM201 3.0 21.9 1.0
C4D A:HEM201 3.0 20.3 1.0
C1B A:HEM201 3.0 25.7 1.0
C4C A:HEM201 3.0 20.4 1.0
C1C A:HEM201 3.0 20.6 1.0
C4A A:HEM201 3.0 23.6 1.0
C1A A:HEM201 3.1 21.0 1.0
CE1 A:HIS18 3.1 18.1 1.0
CD2 A:HIS18 3.1 22.0 1.0
CHD A:HEM201 3.4 21.4 1.0
CHB A:HEM201 3.4 27.1 1.0
CHA A:HEM201 3.4 19.6 1.0
CHC A:HEM201 3.5 22.7 1.0
ND1 A:HIS18 4.2 20.7 1.0
C2D A:HEM201 4.2 19.4 1.0
C3B A:HEM201 4.2 22.5 1.0
C2B A:HEM201 4.2 22.3 1.0
CG A:HIS18 4.2 20.8 1.0
C3D A:HEM201 4.2 22.1 1.0
O A:HOH371 4.3 36.6 1.0
C3C A:HEM201 4.3 19.4 1.0
C3A A:HEM201 4.3 20.1 1.0
C2A A:HEM201 4.3 23.2 1.0
C2C A:HEM201 4.3 21.7 1.0
OH A:TYR67 4.5 25.9 1.0

Reference:

L.J.Mcclelland, H.B.Steele, F.G.Whitby, T.C.Mou, D.Holley, J.B.Ross, S.R.Sprang, B.E.Bowler. Cytochrome C Can Form A Well-Defined Binding Pocket For Hydrocarbons. J. Am. Chem. Soc. V. 138 16770 2016.
ISSN: ESSN 1520-5126
PubMed: 27990813
DOI: 10.1021/JACS.6B10745
Page generated: Tue Aug 6 03:27:14 2024

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