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Potassium in PDB 4xd0: X-Ray Structure of the N-Formyltransferase Qdtf From Providencia Alcalifaciens

Enzymatic activity of X-Ray Structure of the N-Formyltransferase Qdtf From Providencia Alcalifaciens

All present enzymatic activity of X-Ray Structure of the N-Formyltransferase Qdtf From Providencia Alcalifaciens:
2.1.2.9;

Protein crystallography data

The structure of X-Ray Structure of the N-Formyltransferase Qdtf From Providencia Alcalifaciens, PDB code: 4xd0 was solved by J.B.Thoden, C.R.Woodford, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.97 / 1.80
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.134, 78.134, 151.424, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 26.5

Other elements in 4xd0:

The structure of X-Ray Structure of the N-Formyltransferase Qdtf From Providencia Alcalifaciens also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Sodium (Na) 3 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the X-Ray Structure of the N-Formyltransferase Qdtf From Providencia Alcalifaciens (pdb code 4xd0). 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 X-Ray Structure of the N-Formyltransferase Qdtf From Providencia Alcalifaciens, PDB code: 4xd0:

Potassium binding site 1 out of 1 in 4xd0

Go back to Potassium Binding Sites List in 4xd0
Potassium binding site 1 out of 1 in the X-Ray Structure of the N-Formyltransferase Qdtf From Providencia Alcalifaciens


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of X-Ray Structure of the N-Formyltransferase Qdtf From Providencia Alcalifaciens within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K404

b:28.3
occ:1.00
 O A:HOH809 2.2 25.7 1.0
O A:THR260 2.5 16.7 1.0
OG A:SER259 2.7 17.9 1.0
O A:SER241 2.8 30.0 1.0
O A:HOH621 3.0 21.1 1.0
O A:HOH589 3.0 29.9 1.0
O A:SER243 3.1 25.0 1.0
C A:THR260 3.7 18.3 1.0
C A:SER241 3.8 31.3 1.0
N A:THR260 3.9 18.5 1.0
O A:HOH554 3.9 36.6 1.0
CB A:SER259 4.0 19.0 1.0
O A:ASP262 4.1 20.1 1.0
C A:SER243 4.3 30.8 1.0
CA A:THR260 4.4 17.7 1.0
C A:SER259 4.4 18.9 1.0
N A:SER241 4.5 22.9 1.0
CA A:SER259 4.5 19.6 1.0
CA A:SER241 4.5 24.7 1.0
CB A:SER241 4.5 22.1 1.0
C A:LEU242 4.6 28.1 1.0
N A:PRO245 4.7 27.6 1.0
N A:LEU242 4.7 27.3 1.0
N A:ILE261 4.7 16.3 1.0
C A:ILE261 4.7 18.2 1.0
CD A:PRO245 4.7 25.8 1.0
O A:ILE261 4.7 17.3 1.0
N A:SER243 4.7 28.4 1.0
O A:LEU242 4.8 30.0 1.0
CA A:LEU242 4.8 29.4 1.0
CA A:ILE261 4.9 15.6 1.0
C A:LYS240 4.9 26.2 1.0
OD1 A:ASP264 4.9 22.3 1.0
OG A:SER241 4.9 25.9 1.0
O A:HOH535 5.0 20.4 1.0
C A:LYS244 5.0 33.5 1.0

Reference:

C.R.Woodford, J.B.Thoden, H.M.Holden. New Role For the Ankyrin Repeat Revealed By A Study of the N-Formyltransferase From Providencia Alcalifaciens. Biochemistry V. 54 631 2015.
ISSN: ISSN 0006-2960
PubMed: 25574689
DOI: 10.1021/BI501539A
Page generated: Sun Dec 13 23:51:30 2020

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