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Iron in PDB 4cip: Spectroscopically-Validated Structure of Ferrous Cytochrome C Prime From Alcaligenes Xylosoxidans, Reduced Using Ascorbate

Protein crystallography data

The structure of Spectroscopically-Validated Structure of Ferrous Cytochrome C Prime From Alcaligenes Xylosoxidans, Reduced Using Ascorbate, PDB code: 4cip was solved by D.Kekilli, F.Dworkowski, S.Antonyuk, M.A.Hough, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.09 / 1.22
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 53.716, 53.716, 180.624, 90.00, 90.00, 120.00
R / Rfree (%) 14.41 / 17.095

Iron Binding Sites:

The binding sites of Iron atom in the Spectroscopically-Validated Structure of Ferrous Cytochrome C Prime From Alcaligenes Xylosoxidans, Reduced Using Ascorbate (pdb code 4cip). 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 Spectroscopically-Validated Structure of Ferrous Cytochrome C Prime From Alcaligenes Xylosoxidans, Reduced Using Ascorbate, PDB code: 4cip:

Iron binding site 1 out of 1 in 4cip

Go back to Iron Binding Sites List in 4cip
Iron binding site 1 out of 1 in the Spectroscopically-Validated Structure of Ferrous Cytochrome C Prime From Alcaligenes Xylosoxidans, Reduced Using Ascorbate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Spectroscopically-Validated Structure of Ferrous Cytochrome C Prime From Alcaligenes Xylosoxidans, Reduced Using Ascorbate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe128

b:8.9
occ:1.00
FE A:HEC128 0.0 8.9 1.0
NC A:HEC128 2.0 8.8 1.0
NA A:HEC128 2.0 9.1 1.0
ND A:HEC128 2.0 9.3 1.0
NB A:HEC128 2.0 8.9 1.0
NE2 A:HIS120 2.1 9.7 1.0
C4A A:HEC128 3.1 9.0 1.0
C4B A:HEC128 3.1 8.7 1.0
C1B A:HEC128 3.1 9.0 1.0
C1D A:HEC128 3.1 9.5 1.0
C1C A:HEC128 3.1 8.1 1.0
C4C A:HEC128 3.1 8.8 1.0
C4D A:HEC128 3.1 9.4 1.0
C1A A:HEC128 3.1 9.3 1.0
CD2 A:HIS120 3.1 9.9 1.0
CE1 A:HIS120 3.1 11.0 1.0
CHB A:HEC128 3.4 9.9 1.0
CHD A:HEC128 3.4 9.6 1.0
CHC A:HEC128 3.5 8.8 1.0
CHA A:HEC128 3.5 9.1 1.0
CD2 A:LEU16 3.7 9.5 1.0
ND1 A:HIS120 4.2 12.3 1.0
CG A:HIS120 4.3 11.6 1.0
C2B A:HEC128 4.3 9.3 1.0
C3B A:HEC128 4.3 9.2 1.0
C2D A:HEC128 4.3 9.4 1.0
C3C A:HEC128 4.3 8.8 1.0
C2A A:HEC128 4.3 9.6 1.0
C3D A:HEC128 4.3 9.0 1.0
C3A A:HEC128 4.3 9.6 1.0
NH1 A:ARG124 4.3 16.6 0.8
C2C A:HEC128 4.3 8.3 1.0
CD1 A:LEU16 4.4 8.9 1.0
NH1 A:ARG124 4.5 14.3 0.2
CG A:LEU16 4.5 8.7 1.0
CB A:LEU16 4.7 8.8 1.0
CD A:ARG124 4.9 12.9 0.2

Reference:

D.Kekilli, F.S.Dworkowski, G.Pompidor, M.R.Fuchs, C.R.Andrew, S.Antonyuk, R.W.Strange, R.R.Eady, S.S.Hasnain, M.A.Hough. Fingerprinting Redox and Ligand States in Haemprotein Crystal Structures Using Resonance Raman Spectroscopy. Acta Crystallogr.,Sect.D V. 70 1289 2014.
ISSN: ISSN 0907-4449
PubMed: 24816098
DOI: 10.1107/S1399004714004039
Page generated: Sun Dec 13 15:30:14 2020

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