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Potassium in PDB 2b3k: Crystal Structure of Human Methionine Aminopeptidase Type I in the Holo Form

Enzymatic activity of Crystal Structure of Human Methionine Aminopeptidase Type I in the Holo Form

All present enzymatic activity of Crystal Structure of Human Methionine Aminopeptidase Type I in the Holo Form:
3.4.11.18;

Protein crystallography data

The structure of Crystal Structure of Human Methionine Aminopeptidase Type I in the Holo Form, PDB code: 2b3k was solved by A.Addlagatta, X.Hu, J.O.Liu, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.55
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.432, 77.522, 48.308, 90.00, 90.60, 90.00
R / Rfree (%) 19 / 21.5

Other elements in 2b3k:

The structure of Crystal Structure of Human Methionine Aminopeptidase Type I in the Holo Form also contains other interesting chemical elements:

Cobalt (Co) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Human Methionine Aminopeptidase Type I in the Holo Form (pdb code 2b3k). 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 Human Methionine Aminopeptidase Type I in the Holo Form, PDB code: 2b3k:

Potassium binding site 1 out of 1 in 2b3k

Go back to Potassium Binding Sites List in 2b3k
Potassium binding site 1 out of 1 in the Crystal Structure of Human Methionine Aminopeptidase Type I in the Holo Form


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 Human Methionine Aminopeptidase Type I in the Holo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K404

b:30.4
occ:1.00
 O A:VAL209 2.6 14.4 1.0
O A:SER363 2.7 17.4 1.0
O A:HOH588 2.8 23.9 1.0
O A:ASN207 2.9 17.0 1.0
O A:SER205 3.3 14.9 1.0
N A:ASN207 3.6 14.5 1.0
C A:ASN207 3.7 13.2 1.0
C A:VAL209 3.7 12.7 1.0
C A:SER363 3.7 13.1 1.0
C A:VAL206 3.8 15.8 1.0
C A:SER205 3.8 12.2 1.0
CA A:ASN207 4.0 13.7 1.0
O A:VAL206 4.1 15.3 1.0
N A:VAL209 4.2 11.6 1.0
CB A:SER205 4.2 12.7 1.0
N A:VAL206 4.2 11.6 1.0
CA A:VAL206 4.2 13.8 1.0
CA A:VAL209 4.4 15.1 1.0
N A:SER363 4.4 15.7 1.0
CA A:SER363 4.5 13.3 1.0
O A:HOH513 4.5 17.0 1.0
CB A:SER363 4.5 15.5 1.0
CD1 A:ILE225 4.6 24.4 1.0
CA A:SER205 4.6 9.5 1.0
CG1 A:ILE225 4.7 19.6 1.0
CB A:VAL209 4.7 14.8 1.0
N A:ALA364 4.7 12.9 1.0
O A:ILE225 4.8 17.3 1.0
N A:GLU208 4.8 13.0 1.0
N A:ILE210 4.8 12.9 1.0
CA A:ALA364 4.8 12.4 1.0
C A:GLU208 4.8 17.2 1.0
O A:HOH582 4.9 18.7 1.0

Reference:

A.Addlagatta, X.Hu, J.O.Liu, B.W.Matthews. Structural Basis For the Functional Differences Between Type I and Type II Human Methionine Aminopeptidases(,). Biochemistry V. 44 14741 2005.
ISSN: ISSN 0006-2960
PubMed: 16274222
DOI: 10.1021/BI051691K
Page generated: Mon Aug 12 06:05:04 2024

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