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Iron in PDB 5n1t: Crystal Structure of Complex Between Flavocytochrome C and Copper Chaperone Copc From T. Paradoxus

Protein crystallography data

The structure of Crystal Structure of Complex Between Flavocytochrome C and Copper Chaperone Copc From T. Paradoxus, PDB code: 5n1t was solved by E.M.Osipov, A.V.Lilina, T.V.Tikhonova, S.I.Tsallagov, V.O.Popov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 39.530, 138.400, 155.810, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 25.7

Other elements in 5n1t:

The structure of Crystal Structure of Complex Between Flavocytochrome C and Copper Chaperone Copc From T. Paradoxus also contains other interesting chemical elements:

Copper (Cu) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Complex Between Flavocytochrome C and Copper Chaperone Copc From T. Paradoxus (pdb code 5n1t). 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 Complex Between Flavocytochrome C and Copper Chaperone Copc From T. Paradoxus, PDB code: 5n1t:

Iron binding site 1 out of 1 in 5n1t

Go back to Iron Binding Sites List in 5n1t
Iron binding site 1 out of 1 in the Crystal Structure of Complex Between Flavocytochrome C and Copper Chaperone Copc From T. Paradoxus


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 Complex Between Flavocytochrome C and Copper Chaperone Copc From T. Paradoxus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe901

b:39.4
occ:1.00
FE B:HEC901 0.0 39.4 1.0
NE2 B:HIS15 1.9 39.1 1.0
ND B:HEC901 2.1 40.8 1.0
NA B:HEC901 2.1 46.1 1.0
NB B:HEC901 2.1 43.9 1.0
NC B:HEC901 2.1 44.6 1.0
SD B:MET53 2.3 41.5 1.0
CD2 B:HIS15 2.8 34.7 1.0
CE1 B:HIS15 3.0 36.4 1.0
C1D B:HEC901 3.0 42.3 1.0
C4C B:HEC901 3.1 42.7 1.0
C4A B:HEC901 3.1 47.9 1.0
C1B B:HEC901 3.1 41.1 1.0
C4D B:HEC901 3.1 46.2 1.0
C1A B:HEC901 3.1 49.6 1.0
C1C B:HEC901 3.1 44.6 1.0
C4B B:HEC901 3.1 47.0 1.0
CHD B:HEC901 3.4 43.3 1.0
CHB B:HEC901 3.4 42.7 1.0
CG B:MET53 3.5 44.8 1.0
CE B:MET53 3.5 40.5 1.0
CHA B:HEC901 3.5 49.2 1.0
CHC B:HEC901 3.5 44.3 1.0
CG B:HIS15 4.0 36.4 1.0
ND1 B:HIS15 4.0 37.3 1.0
C2D B:HEC901 4.4 44.5 1.0
C3C B:HEC901 4.4 46.7 1.0
C3D B:HEC901 4.4 47.0 1.0
C3A B:HEC901 4.4 48.9 1.0
C2B B:HEC901 4.4 43.3 1.0
C2A B:HEC901 4.4 50.2 1.0
C3B B:HEC901 4.4 46.1 1.0
C2C B:HEC901 4.5 43.3 1.0
CB B:MET53 4.9 43.5 1.0

Reference:

E.M.Osipov, A.V.Lilina, S.I.Tsallagov, T.N.Safonova, D.Y.Sorokin, T.V.Tikhonova, V.O.Popov. Structure of the Flavocytochrome C Sulfide Dehydrogenase Associated with the Copper-Binding Protein Copc From the Haloalkaliphilic Sulfur-Oxidizing Bacterium Thioalkalivibrio Paradoxusarh 1. Acta Crystallogr D Struct V. 74 632 2018BIOL.
ISSN: ISSN 2059-7983
PubMed: 29968673
DOI: 10.1107/S2059798318005648
Page generated: Tue Aug 6 06:03:13 2024

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