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Potassium in PDB 4c6v: Crystal Structure of M. Tuberculosis Kasa in Complex with TLM5 (Soak For 5 Min)

Enzymatic activity of Crystal Structure of M. Tuberculosis Kasa in Complex with TLM5 (Soak For 5 Min)

All present enzymatic activity of Crystal Structure of M. Tuberculosis Kasa in Complex with TLM5 (Soak For 5 Min):
2.3.1.41;

Protein crystallography data

The structure of Crystal Structure of M. Tuberculosis Kasa in Complex with TLM5 (Soak For 5 Min), PDB code: 4c6v was solved by J.Schiebel, K.Kapilashrami, A.Fekete, G.R.Bommineni, C.M.Schaefer, M.J.Mueller, P.J.Tonge, C.Kisker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 66.88 / 2.70
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 77.230, 77.230, 146.851, 90.00, 90.00, 120.00
R / Rfree (%) 17.643 / 24.217

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of M. Tuberculosis Kasa in Complex with TLM5 (Soak For 5 Min) (pdb code 4c6v). 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 M. Tuberculosis Kasa in Complex with TLM5 (Soak For 5 Min), PDB code: 4c6v:

Potassium binding site 1 out of 1 in 4c6v

Go back to Potassium Binding Sites List in 4c6v
Potassium binding site 1 out of 1 in the Crystal Structure of M. Tuberculosis Kasa in Complex with TLM5 (Soak For 5 Min)


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 M. Tuberculosis Kasa in Complex with TLM5 (Soak For 5 Min) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1418

b:46.2
occ:1.00
OE1 A:GLU354 2.5 28.0 1.0
OD1 A:ASN399 2.5 33.0 1.0
O A:ASN309 2.6 29.9 1.0
O A:ASN400 2.7 31.2 1.0
OD1 A:ASN309 2.8 33.1 1.0
O A:ALA310 2.9 29.2 1.0
C A:ALA310 3.2 29.2 1.0
C A:ASN309 3.3 29.7 1.0
CD A:GLU354 3.6 27.7 1.0
N A:HIS311 3.6 29.0 1.0
CG A:ASN399 3.7 30.2 1.0
CB A:GLU354 3.7 22.9 1.0
CG A:ASN309 3.7 32.1 1.0
C A:ASN400 3.8 31.7 1.0
N A:ASN400 3.8 31.5 1.0
CA A:HIS311 3.9 28.4 1.0
N A:ALA310 3.9 29.8 1.0
CA A:ALA310 4.0 29.9 1.0
CB A:ASN309 4.1 29.8 1.0
CG A:GLU354 4.2 24.4 1.0
CA A:ASN309 4.3 30.9 1.0
CA A:ASN400 4.3 31.8 1.0
ND2 A:ASN399 4.4 29.5 1.0
C A:ASN399 4.5 31.4 1.0
OE2 A:GLU354 4.5 29.3 1.0
CA A:ASN399 4.7 31.2 1.0
CB A:ASN400 4.8 31.9 1.0
CB A:ASN399 4.8 30.2 1.0
ND2 A:ASN309 4.9 35.0 1.0
CB A:HIS311 4.9 27.3 1.0
C A:HIS311 4.9 29.5 1.0
N A:SER401 4.9 32.9 1.0

Reference:

J.Schiebel, K.Kapilashrami, A.Fekete, G.R.Bommineni, C.M.Schaefer, M.J.Mueller, P.J.Tonge, C.Kisker. Structural Basis For the Recognition of Mycolic Acid Precursors By Kasa, A Condensing Enzyme and Drug Target From Mycobacterium Tuberculosis J.Biol.Chem. V. 288 34190 2013.
ISSN: ISSN 0021-9258
PubMed: 24108128
DOI: 10.1074/JBC.M113.511436
Page generated: Sun Dec 13 23:29:22 2020

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