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Potassium in PDB 8adq: Crystal Structure of Holo-Swhpa-Mg (Hydroxy Ketone Aldolase) From Sphingomonas Wittichii RW1 in Complex with Hydroxypyruvate and D- Glyceraldehyde

Protein crystallography data

The structure of Crystal Structure of Holo-Swhpa-Mg (Hydroxy Ketone Aldolase) From Sphingomonas Wittichii RW1 in Complex with Hydroxypyruvate and D- Glyceraldehyde, PDB code: 8adq was solved by I.Justo, S.R.Marsden, U.Hanefeld, I.Bento, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.90 / 1.60
Space group P 42 3 2
Cell size a, b, c (Å), α, β, γ (°) 115.793, 115.793, 115.793, 90, 90, 90
R / Rfree (%) 16.8 / 20.1

Other elements in 8adq:

The structure of Crystal Structure of Holo-Swhpa-Mg (Hydroxy Ketone Aldolase) From Sphingomonas Wittichii RW1 in Complex with Hydroxypyruvate and D- Glyceraldehyde also contains other interesting chemical elements:

Bromine (Br) 3 atoms
Magnesium (Mg) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Holo-Swhpa-Mg (Hydroxy Ketone Aldolase) From Sphingomonas Wittichii RW1 in Complex with Hydroxypyruvate and D- Glyceraldehyde (pdb code 8adq). 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 Structure of Holo-Swhpa-Mg (Hydroxy Ketone Aldolase) From Sphingomonas Wittichii RW1 in Complex with Hydroxypyruvate and D- Glyceraldehyde, PDB code: 8adq:

Potassium binding site 1 out of 1 in 8adq

Go back to Potassium Binding Sites List in 8adq
Potassium binding site 1 out of 1 in the Crystal Structure of Holo-Swhpa-Mg (Hydroxy Ketone Aldolase) From Sphingomonas Wittichii RW1 in Complex with Hydroxypyruvate and D- Glyceraldehyde


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Holo-Swhpa-Mg (Hydroxy Ketone Aldolase) From Sphingomonas Wittichii RW1 in Complex with Hydroxypyruvate and D- Glyceraldehyde within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K313

b:29.4
occ:1.00
O A:ALA31 2.6 32.6 1.0
O A:LEU33 2.6 33.0 1.0
O A:HOH593 2.7 39.9 1.0
O A:TYR35 2.8 31.1 1.0
O A:HOH545 2.9 37.9 1.0
O A:GLY63 2.9 35.1 1.0
HB2 A:ALA64 3.4 39.1 1.0
H A:TYR35 3.5 36.9 1.0
C A:GLY63 3.7 35.4 1.0
C A:ALA31 3.8 32.3 1.0
C A:LEU33 3.9 32.4 1.0
HA A:ARG32 3.9 36.8 1.0
C A:TYR35 3.9 32.1 1.0
HA A:ASP34 3.9 40.0 1.0
HA A:ALA64 4.0 37.2 1.0
N A:TYR35 4.0 30.8 1.0
HZ3 A:LYS3 4.2 77.7 1.0
N A:ALA64 4.2 32.2 1.0
HA3 A:GLY63 4.2 41.0 1.0
CB A:ALA64 4.2 32.6 1.0
C A:ARG32 4.2 31.3 1.0
HB2 A:TYR35 4.3 36.5 1.0
O A:HOH440 4.3 34.8 1.0
CA A:ALA64 4.4 31.0 1.0
CA A:ARG32 4.4 30.7 1.0
N A:LEU33 4.4 31.0 1.0
HE2 A:LYS3 4.5 67.7 1.0
HZ1 A:LYS3 4.5 77.7 1.0
CA A:TYR35 4.5 31.6 1.0
O A:ARG32 4.5 34.2 1.0
O A:GLY62 4.5 35.2 1.0
CA A:GLY63 4.6 34.2 1.0
N A:ARG32 4.6 31.5 1.0
CA A:ASP34 4.6 33.3 1.0
HA A:ASP36 4.6 36.9 1.0
HA A:ALA31 4.6 36.4 1.0
N A:ASP34 4.7 32.3 1.0
HB1 A:ALA64 4.7 39.1 1.0
H A:LEU33 4.7 37.2 1.0
NZ A:LYS3 4.7 64.8 1.0
C A:ASP34 4.7 35.3 1.0
CA A:LEU33 4.8 31.6 1.0
CA A:ALA31 4.8 30.3 1.0
H A:ALA64 4.9 38.6 1.0
HB3 A:ALA64 4.9 39.1 1.0
CB A:TYR35 4.9 30.4 1.0
N A:ASP36 5.0 32.3 1.0

Reference:

S.R.Marsden, H.J.Wijma, M.K.F.Mohr, I.Justo, P.L.Hagedoorn, J.Laustsen, C.M.Jeffries, D.Svergun, L.Mestrom, D.G.G.Mcmillan, I.Bento, U.Hanefeld. Substrate Induced Movement of the Metal Cofactor Between Active and Resting State. Angew.Chem.Int.Ed.Engl. V. 61 13338 2022.
ISSN: ESSN 1521-3773
PubMed: 36214476
DOI: 10.1002/ANIE.202213338
Page generated: Mon Aug 12 22:00:40 2024

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