Atomistry » Potassium » PDB 5x24-5ze2 » 5yr4
Atomistry »
  Potassium »
    PDB 5x24-5ze2 »
      5yr4 »

Potassium in PDB 5yr4: Human Methionine Aminopeptidase Type 1B (F309M Mutant) in Complex with TNP470

Enzymatic activity of Human Methionine Aminopeptidase Type 1B (F309M Mutant) in Complex with TNP470

All present enzymatic activity of Human Methionine Aminopeptidase Type 1B (F309M Mutant) in Complex with TNP470:
3.4.11.18;

Protein crystallography data

The structure of Human Methionine Aminopeptidase Type 1B (F309M Mutant) in Complex with TNP470, PDB code: 5yr4 was solved by T.Arya, V.Pillalamarri, A.Addlagatta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.58 / 1.82
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.210, 77.241, 47.174, 90.00, 92.03, 90.00
R / Rfree (%) 17.3 / 22.7

Other elements in 5yr4:

The structure of Human Methionine Aminopeptidase Type 1B (F309M Mutant) in Complex with TNP470 also contains other interesting chemical elements:

Cobalt (Co) 4 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Human Methionine Aminopeptidase Type 1B (F309M Mutant) in Complex with TNP470 (pdb code 5yr4). 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 Human Methionine Aminopeptidase Type 1B (F309M Mutant) in Complex with TNP470, PDB code: 5yr4:

Potassium binding site 1 out of 1 in 5yr4

Go back to Potassium Binding Sites List in 5yr4
Potassium binding site 1 out of 1 in the Human Methionine Aminopeptidase Type 1B (F309M Mutant) in Complex with TNP470


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Human Methionine Aminopeptidase Type 1B (F309M Mutant) in Complex with TNP470 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K405

b:24.6
occ:1.00
 O A:VAL209 2.6 22.1 1.0
O A:SER363 2.6 25.2 1.0
O A:HOH436 2.8 21.4 1.0
O A:ASN207 2.8 23.5 1.0
O A:SER205 3.0 21.2 1.0
N A:ASN207 3.6 23.5 1.0
C A:ASN207 3.6 24.4 1.0
C A:SER363 3.7 24.1 1.0
C A:SER205 3.7 21.9 1.0
C A:VAL209 3.7 22.2 1.0
C A:VAL206 3.7 21.9 1.0
O A:VAL206 4.0 23.0 1.0
CA A:ASN207 4.0 23.4 1.0
CB A:SER205 4.2 21.3 1.0
N A:VAL206 4.2 23.2 1.0
N A:VAL209 4.3 24.6 1.0
CA A:VAL206 4.3 24.9 1.0
O A:HOH421 4.4 20.3 1.0
N A:SER363 4.4 25.7 1.0
CA A:SER363 4.5 25.4 1.0
CA A:VAL209 4.5 22.0 1.0
CA A:SER205 4.6 20.1 1.0
N A:ALA364 4.6 22.8 1.0
CG1 A:ILE225 4.6 25.8 1.0
CB A:SER363 4.6 25.0 1.0
CD1 A:ILE225 4.7 27.2 1.0
N A:GLU208 4.7 24.8 1.0
O A:ILE225 4.7 24.7 1.0
CA A:ALA364 4.7 22.5 1.0
N A:ILE210 4.7 22.6 1.0
CB A:VAL209 4.9 22.9 1.0
N A:ASN227 4.9 22.2 1.0
C A:GLU208 4.9 25.3 1.0
O A:HOH428 4.9 22.2 1.0
CB A:ASN227 4.9 19.5 1.0
CA A:ILE210 5.0 24.8 1.0

Reference:

V.Pillalamarri, T.Arya, N.Haque, S.C.Bala, A.K.Marapaka, A.Addlagatta. Discovery of Natural Product Ovalicin Sensitive Type 1 Methionine Aminopeptidases: Molecular and Structural Basis. Biochem. J. V. 476 991 2019.
ISSN: ESSN 1470-8728
PubMed: 30837307
DOI: 10.1042/BCJ20180874
Page generated: Mon Aug 12 15:14:28 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy