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Iron in PDB 6rxn: The Structure of Rubredoxin From Desulfovibrio Desulfuricans

Protein crystallography data

The structure of The Structure of Rubredoxin From Desulfovibrio Desulfuricans, PDB code: 6rxn was solved by R.E.Stenkamp, L.C.Sieker, L.H.Jensen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 5.00 / 1.50
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 24.920, 17.790, 19.720, 101.00, 83.40, 104.50
R / Rfree (%) n/a / n/a

Iron Binding Sites:

The binding sites of Iron atom in the The Structure of Rubredoxin From Desulfovibrio Desulfuricans (pdb code 6rxn). 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 The Structure of Rubredoxin From Desulfovibrio Desulfuricans, PDB code: 6rxn:

Iron binding site 1 out of 1 in 6rxn

Go back to Iron Binding Sites List in 6rxn
Iron binding site 1 out of 1 in the The Structure of Rubredoxin From Desulfovibrio Desulfuricans


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Structure of Rubredoxin From Desulfovibrio Desulfuricans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe53

b:6.9
occ:1.00
SG A:CYS42 2.2 6.2 1.0
SG A:CYS9 2.3 6.5 1.0
SG A:CYS6 2.3 6.2 1.0
SG A:CYS39 2.3 5.0 1.0
CB A:CYS6 3.2 4.3 1.0
CB A:CYS39 3.3 3.7 1.0
CB A:CYS9 3.3 7.4 1.0
CB A:CYS42 3.3 6.2 1.0
N A:CYS42 3.8 4.8 1.0
N A:CYS9 3.8 4.4 1.0
CA A:CYS42 4.1 4.7 1.0
CA A:CYS9 4.2 5.5 1.0
CG2 A:VAL44 4.2 6.5 1.0
CB A:TYR11 4.5 4.9 1.0
CA A:CYS6 4.6 3.8 1.0
CA A:CYS39 4.7 4.5 1.0
CB A:VAL41 4.7 7.4 1.0
CB A:VAL8 4.7 7.3 1.0
C A:CYS42 4.7 6.2 1.0
C A:VAL41 4.8 6.6 1.0
C A:CYS9 4.8 5.6 1.0
N A:GLY43 4.8 4.8 1.0
C A:VAL8 4.8 6.5 1.0
N A:TYR11 4.9 5.2 1.0
N A:GLY10 5.0 5.8 1.0
CZ A:PHE49 5.0 6.8 1.0

Reference:

R.E.Stenkamp, L.C.Sieker, L.H.Jensen. The Structure of Rubredoxin From Desulfovibrio Desulfuricans Strain 27774 at 1.5 A Resolution. Proteins V. 8 352 1990.
ISSN: ISSN 0887-3585
PubMed: 2091025
DOI: 10.1002/PROT.340080409
Page generated: Sun Dec 13 17:04:28 2020

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