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Potassium in PDB 1fqe: Crystal Structures of Mutant (K206A) That Abolish the Dilysine Interaction in the N-Lobe of Human Transferrin

Protein crystallography data

The structure of Crystal Structures of Mutant (K206A) That Abolish the Dilysine Interaction in the N-Lobe of Human Transferrin, PDB code: 1fqe was solved by D.Nurizzo, H.M.Baker, E.N.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.73 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.900, 57.300, 135.900, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 23.7

Other elements in 1fqe:

The structure of Crystal Structures of Mutant (K206A) That Abolish the Dilysine Interaction in the N-Lobe of Human Transferrin also contains other interesting chemical elements:

Iron (Fe) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structures of Mutant (K206A) That Abolish the Dilysine Interaction in the N-Lobe of Human Transferrin (pdb code 1fqe). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Crystal Structures of Mutant (K206A) That Abolish the Dilysine Interaction in the N-Lobe of Human Transferrin, PDB code: 1fqe:

Potassium binding site 1 out of 1 in 1fqe

Go back to Potassium Binding Sites List in 1fqe
Potassium binding site 1 out of 1 in the Crystal Structures of Mutant (K206A) That Abolish the Dilysine Interaction in the N-Lobe of Human Transferrin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structures of Mutant (K206A) That Abolish the Dilysine Interaction in the N-Lobe of Human Transferrin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K700

b:18.8
occ:1.00
O A:PHE154 2.7 12.1 1.0
O A:HOH799 2.7 21.3 1.0
O A:ASN152 2.9 10.7 1.0
OE1 A:GLN169 3.0 16.6 1.0
O A:ALA151 3.0 9.5 1.0
O A:HOH846 3.2 30.9 1.0
C A:ASN152 3.4 10.8 1.0
CD A:GLN169 3.5 16.3 1.0
CA A:ASN152 3.5 11.2 1.0
NE2 A:GLN169 3.5 17.2 1.0
C A:PHE154 3.9 11.8 1.0
C A:ALA151 3.9 9.9 1.0
N A:ASN152 4.2 10.5 1.0
O A:HOH807 4.3 20.2 1.0
CA A:SER155 4.3 12.8 1.0
O A:HOH998 4.3 35.7 1.0
O A:HOH949 4.5 31.3 1.0
N A:PHE153 4.5 10.7 1.0
O A:HOH886 4.5 26.0 1.0
N A:SER155 4.6 11.7 1.0
O A:HOH818 4.6 20.3 1.0
ND2 A:ASN152 4.7 13.1 1.0
CB A:ASN152 4.7 12.0 1.0
CG A:GLN169 4.7 15.5 1.0
N A:PHE154 4.7 10.3 1.0
C A:PHE153 4.8 10.6 1.0
O A:HOH730 4.9 9.7 1.0
CA A:PHE154 5.0 11.1 1.0

Reference:

D.Nurizzo, H.M.Baker, Q.Y.He, R.T.Macgillivray, A.B.Mason, R.C.Woodworth, E.N.Baker. Crystal Structures and Iron Release Properties of Mutants (K206A and K296A) That Abolish the Dilysine Interaction in the N-Lobe of Human Transferrin. Biochemistry V. 40 1616 2001.
ISSN: ISSN 0006-2960
PubMed: 11327820
DOI: 10.1021/BI002050M
Page generated: Sun Dec 13 22:42:58 2020

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