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Iron in PDB 3de9: Crystal Structure of A Trimeric Cytochrome CB562 Assembly Induced By Nickel Coordination

Protein crystallography data

The structure of Crystal Structure of A Trimeric Cytochrome CB562 Assembly Induced By Nickel Coordination, PDB code: 3de9 was solved by E.N.Salgado, R.A.Lewis, A.L.Rheingold, F.A.Tezcan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.52 / 2.04
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 51.042, 51.042, 121.971, 90.00, 90.00, 120.00
R / Rfree (%) 21.7 / 27.8

Other elements in 3de9:

The structure of Crystal Structure of A Trimeric Cytochrome CB562 Assembly Induced By Nickel Coordination also contains other interesting chemical elements:

Nickel (Ni) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of A Trimeric Cytochrome CB562 Assembly Induced By Nickel Coordination (pdb code 3de9). 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 Trimeric Cytochrome CB562 Assembly Induced By Nickel Coordination, PDB code: 3de9:

Iron binding site 1 out of 1 in 3de9

Go back to Iron Binding Sites List in 3de9
Iron binding site 1 out of 1 in the Crystal Structure of A Trimeric Cytochrome CB562 Assembly Induced By Nickel Coordination


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 Trimeric Cytochrome CB562 Assembly Induced By Nickel Coordination within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe150

b:33.0
occ:1.00
FE A:HEM150 0.0 33.0 1.0
NE2 A:HIS102 2.0 34.7 1.0
NB A:HEM150 2.0 31.1 1.0
NA A:HEM150 2.0 36.8 1.0
ND A:HEM150 2.1 33.5 1.0
NC A:HEM150 2.2 31.0 1.0
SD A:MET7 2.3 27.4 1.0
CE1 A:HIS102 2.9 33.2 1.0
C1A A:HEM150 3.0 36.3 1.0
C4B A:HEM150 3.0 29.3 1.0
C1B A:HEM150 3.0 33.4 1.0
C4D A:HEM150 3.0 35.6 1.0
C4A A:HEM150 3.1 37.9 1.0
CD2 A:HIS102 3.1 34.0 1.0
C1C A:HEM150 3.1 27.8 1.0
C1D A:HEM150 3.2 33.0 1.0
C4C A:HEM150 3.2 27.7 1.0
CHA A:HEM150 3.3 35.8 1.0
CE A:MET7 3.3 29.1 1.0
CHC A:HEM150 3.4 27.7 1.0
CHB A:HEM150 3.4 34.7 1.0
CG A:MET7 3.5 31.1 1.0
CHD A:HEM150 3.6 31.6 1.0
ND1 A:HIS102 4.1 32.7 1.0
CB A:MET7 4.1 30.9 1.0
CG A:HIS102 4.2 33.8 1.0
C2A A:HEM150 4.2 39.5 1.0
C3B A:HEM150 4.2 28.9 1.0
C2B A:HEM150 4.2 31.3 1.0
C3A A:HEM150 4.2 38.8 1.0
C3D A:HEM150 4.3 35.4 1.0
C2C A:HEM150 4.4 24.2 1.0
C3C A:HEM150 4.4 24.5 1.0
C2D A:HEM150 4.4 34.3 1.0
CA A:MET7 5.0 31.5 1.0

Reference:

E.N.Salgado, R.A.Lewis, S.Mossin, A.L.Rheingold, F.A.Tezcan. Control of Protein Oligomerization Symmetry By Metal Coordination: C2 and C3 Symmetrical Assemblies Through Cu(II) and Ni(II) Coordination. Inorg.Chem. V. 48 2726 2009.
ISSN: ISSN 0020-1669
PubMed: 19267481
DOI: 10.1021/IC9001237
Page generated: Sun Dec 13 15:03:37 2020

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