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Potassium in PDB 2b3l: Crystal Structure of Type I Human Methionine Aminopeptidase in the Apo Form

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

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

Protein crystallography data

The structure of Crystal Structure of Type I Human Methionine Aminopeptidase in the Apo Form, PDB code: 2b3l 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) 50.00 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.217, 77.276, 47.850, 90.00, 91.59, 90.00
R / Rfree (%) 11.1 / 18

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Type I Human Methionine Aminopeptidase in the Apo Form (pdb code 2b3l). 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 Type I Human Methionine Aminopeptidase in the Apo Form, PDB code: 2b3l:

Potassium binding site 1 out of 1 in 2b3l

Go back to Potassium Binding Sites List in 2b3l
Potassium binding site 1 out of 1 in the Crystal Structure of Type I Human Methionine Aminopeptidase in the Apo 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 Type I Human Methionine Aminopeptidase in the Apo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K403

b:23.3
occ:1.00
O A:HOH768 2.4 26.4 0.5
O A:VAL209 2.6 14.1 1.0
O A:SER363 2.7 14.9 1.0
O A:HOH665 2.8 16.6 1.0
O A:ASN207 2.9 15.5 1.0
O A:SER205 3.2 15.1 1.0
N A:ASN207 3.5 12.5 1.0
C A:VAL206 3.7 11.9 1.0
C A:VAL209 3.7 11.3 1.0
C A:SER363 3.7 12.5 1.0
C A:ASN207 3.7 14.2 1.0
C A:SER205 3.8 11.2 1.0
O A:VAL206 4.0 14.0 1.0
CA A:ASN207 4.1 14.0 1.0
CB A:SER205 4.2 11.2 1.0
N A:VAL206 4.3 10.2 1.0
N A:VAL209 4.3 12.5 1.0
CA A:VAL206 4.3 11.5 1.0
O A:HOH506 4.4 15.4 1.0
N A:SER363 4.4 13.5 1.0
CA A:VAL209 4.5 11.3 1.0
CA A:SER363 4.5 14.1 1.0
CB A:SER363 4.6 15.2 1.0
CA A:SER205 4.6 10.1 1.0
CG1 A:ILE225 4.6 17.3 1.0
N A:ALA364 4.6 12.1 1.0
CB A:VAL209 4.7 11.8 1.0
CA A:ALA364 4.7 11.7 1.0
N A:ILE210 4.7 11.3 1.0
O A:ILE225 4.8 13.6 1.0
CD1 A:ILE225 4.8 17.1 1.0
N A:GLU208 4.8 13.7 1.0
C A:GLU208 4.9 11.5 1.0
O A:HOH505 4.9 14.8 1.0
N A:ASN227 4.9 9.7 1.0
CB A:ASN227 5.0 10.5 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: Sun Dec 13 23:08:57 2020

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