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Iron in PDB 3fgs: Crystal Structure of G65R/K206E Double Mutant of the N-Lobe Human Transferrin

Protein crystallography data

The structure of Crystal Structure of G65R/K206E Double Mutant of the N-Lobe Human Transferrin, PDB code: 3fgs was solved by P.J.Halbrooks, A.B.Mason, S.J.Everse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.49 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.347, 57.056, 133.737, 90.00, 90.00, 90.00
R / Rfree (%) 21.6 / 24.6

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of G65R/K206E Double Mutant of the N-Lobe Human Transferrin (pdb code 3fgs). 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 G65R/K206E Double Mutant of the N-Lobe Human Transferrin, PDB code: 3fgs:

Iron binding site 1 out of 1 in 3fgs

Go back to Iron Binding Sites List in 3fgs
Iron binding site 1 out of 1 in the Crystal Structure of G65R/K206E Double Mutant of the N-Lobe Human Transferrin


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 G65R/K206E Double Mutant of the N-Lobe Human Transferrin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe402

b:11.5
occ:1.00
OH A:TYR188 2.1 8.7 1.0
OH A:TYR95 2.1 8.0 1.0
NE2 A:HIS249 2.2 8.5 1.0
OD1 A:ASP63 2.2 7.7 1.0
O1 A:CO3401 2.3 11.8 1.0
O2 A:CO3401 2.4 12.6 1.0
C A:CO3401 2.7 9.9 1.0
CD2 A:HIS249 3.0 10.0 1.0
CZ A:TYR188 3.1 9.7 1.0
CZ A:TYR95 3.1 8.8 1.0
CE1 A:HIS249 3.2 9.2 1.0
CG A:ASP63 3.3 8.6 1.0
CE2 A:TYR95 3.7 8.1 1.0
CB A:ASP63 3.8 8.3 1.0
CE1 A:TYR188 3.9 9.0 1.0
CE2 A:TYR188 4.0 8.6 1.0
O A:HOH545 4.0 15.4 1.0
O3 A:CO3401 4.0 11.2 1.0
CE1 A:TYR95 4.2 8.9 1.0
CG A:HIS249 4.2 9.4 1.0
ND1 A:HIS249 4.3 10.2 1.0
OD2 A:ASP63 4.3 8.6 1.0
NZ A:LYS296 4.3 7.4 1.0
CA A:ASP63 4.4 8.2 1.0
NH2 A:ARG124 4.5 14.9 1.0
CB A:SER125 4.6 11.8 1.0
NE A:ARG124 4.8 13.1 1.0
N A:ALA126 4.8 10.4 1.0
CD A:LYS296 4.9 8.6 1.0
N A:SER125 4.9 10.3 1.0
CE A:LYS296 5.0 8.2 1.0
CD2 A:TYR95 5.0 6.2 1.0

Reference:

A.B.Mason, P.J.Halbrooks, N.G.James, S.L.Byrne, J.K.Grady, N.D.Chasteen, C.E.Bobst, I.A.Kaltashov, V.C.Smith, R.T.Macgillivray, S.J.Everse. Structural and Functional Consequences of the Substitution of Glycine 65 with Arginine in the N-Lobe of Human Transferrin. Biochemistry V. 48 1945 2009.
ISSN: ISSN 0006-2960
PubMed: 19219998
DOI: 10.1021/BI802254X
Page generated: Sun Dec 13 15:05:36 2020

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