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Iron in PDB 4cda: Spectroscopically-Validated Structure of Ferric Cytochrome C Prime From Alcaligenes Xylosoxidans

Protein crystallography data

The structure of Spectroscopically-Validated Structure of Ferric Cytochrome C Prime From Alcaligenes Xylosoxidans, PDB code: 4cda 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) 46.21 / 1.30
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 53.354, 53.354, 180.992, 90.00, 90.00, 120.00
R / Rfree (%) 15.44 / 17.935

Iron Binding Sites:

The binding sites of Iron atom in the Spectroscopically-Validated Structure of Ferric Cytochrome C Prime From Alcaligenes Xylosoxidans (pdb code 4cda). 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 Ferric Cytochrome C Prime From Alcaligenes Xylosoxidans, PDB code: 4cda:

Iron binding site 1 out of 1 in 4cda

Go back to Iron Binding Sites List in 4cda
Iron binding site 1 out of 1 in the Spectroscopically-Validated Structure of Ferric Cytochrome C Prime From Alcaligenes Xylosoxidans


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 Ferric Cytochrome C Prime From Alcaligenes Xylosoxidans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe129

b:8.4
occ:1.00
FE A:HEC129 0.0 8.4 1.0
ND A:HEC129 2.0 8.1 1.0
NA A:HEC129 2.0 8.1 1.0
NB A:HEC129 2.0 8.2 1.0
NE2 A:HIS120 2.0 8.9 1.0
NC A:HEC129 2.1 9.0 1.0
CD2 A:HIS120 3.0 8.2 1.0
C4B A:HEC129 3.0 8.4 1.0
CE1 A:HIS120 3.0 9.0 1.0
C1A A:HEC129 3.1 8.1 1.0
C1C A:HEC129 3.1 9.2 1.0
C4D A:HEC129 3.1 7.6 1.0
C1B A:HEC129 3.1 8.0 1.0
C1D A:HEC129 3.1 7.6 1.0
C4A A:HEC129 3.1 8.1 1.0
C4C A:HEC129 3.1 7.6 1.0
CHC A:HEC129 3.4 8.9 1.0
CHA A:HEC129 3.4 7.5 1.0
CHD A:HEC129 3.4 8.6 1.0
CHB A:HEC129 3.5 9.6 1.0
CD2 A:LEU16 3.8 6.5 1.0
ND1 A:HIS120 4.1 9.6 1.0
CG A:HIS120 4.2 9.6 1.0
C3B A:HEC129 4.3 8.4 1.0
C2D A:HEC129 4.3 6.8 1.0
C2B A:HEC129 4.3 8.2 1.0
C2A A:HEC129 4.3 8.0 1.0
C3D A:HEC129 4.3 7.5 1.0
C3A A:HEC129 4.3 7.7 1.0
C2C A:HEC129 4.3 8.0 1.0
C3C A:HEC129 4.3 7.7 1.0
CD1 A:LEU16 4.5 7.0 1.0
CG A:LEU16 4.5 6.6 1.0
NH1 A:ARG124 4.7 13.8 1.0
CB A:LEU16 4.8 6.2 1.0

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: Mon Aug 5 00:34:59 2024

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