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Iron in PDB 1b2j: Clostridium Pasteurianum Rubredoxin G43A Mutant

Protein crystallography data

The structure of Clostridium Pasteurianum Rubredoxin G43A Mutant, PDB code: 1b2j was solved by M.J.Maher, J.M.Guss, M.C.J.Wilce, A.G.Wedd, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.60
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 64.380, 64.380, 32.850, 90.00, 90.00, 120.00
R / Rfree (%) 18.3 / 23.4

Iron Binding Sites:

The binding sites of Iron atom in the Clostridium Pasteurianum Rubredoxin G43A Mutant (pdb code 1b2j). 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 Clostridium Pasteurianum Rubredoxin G43A Mutant, PDB code: 1b2j:

Iron binding site 1 out of 1 in 1b2j

Go back to Iron Binding Sites List in 1b2j
Iron binding site 1 out of 1 in the Clostridium Pasteurianum Rubredoxin G43A Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Clostridium Pasteurianum Rubredoxin G43A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe55

b:18.6
occ:1.00
SG A:CYS42 2.2 21.9 1.0
SG A:CYS9 2.2 17.6 1.0
SG A:CYS39 2.3 17.1 1.0
SG A:CYS6 2.4 17.1 1.0
CB A:CYS6 3.2 15.8 1.0
CB A:CYS39 3.2 16.9 1.0
CB A:CYS9 3.3 18.3 1.0
CB A:CYS42 3.3 19.5 1.0
N A:CYS42 3.7 23.1 1.0
N A:CYS9 3.9 16.6 1.0
CA A:CYS9 4.1 17.0 1.0
CA A:CYS42 4.1 23.4 1.0
CB A:TYR11 4.4 17.8 1.0
CG2 A:VAL44 4.5 21.4 1.0
C A:CYS9 4.6 18.2 1.0
CA A:CYS6 4.7 13.3 1.0
CA A:CYS39 4.7 17.6 1.0
C A:LEU41 4.7 24.2 1.0
CB A:VAL8 4.7 21.8 1.0
C A:CYS42 4.8 24.0 1.0
C A:VAL8 4.8 19.7 1.0
N A:GLY10 4.8 17.0 1.0
CB A:LEU41 4.8 28.1 1.0
N A:TYR11 4.9 16.2 1.0
N A:ALA43 4.9 22.5 1.0

Reference:

M.J.Maher, Z.Xiao, M.C.Wilce, J.M.Guss, A.G.Wedd. Rubredoxin From Clostridium Pasteurianum. Structures of G10A, G43A and G10VG43A Mutant Proteins. Mutation of Conserved Glycine 10 to Valine Causes the 9-10 Peptide Link to Invert. Acta Crystallogr.,Sect.D V. 55 962 1999.
ISSN: ISSN 0907-4449
PubMed: 10216292
DOI: 10.1107/S0907444999001900
Page generated: Sat Aug 3 02:29:24 2024

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