Atomistry » Manganese » PDB 3hw6-3ki9 » 3iu7
Atomistry »
  Manganese »
    PDB 3hw6-3ki9 »
      3iu7 »

Manganese in PDB 3iu7: M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02

Enzymatic activity of M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02

All present enzymatic activity of M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02:
3.4.11.18;

Protein crystallography data

The structure of M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02, PDB code: 3iu7 was solved by Q.Z.Ye, J.P.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 21.14 / 1.40
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 106.412, 106.412, 50.422, 90.00, 90.00, 120.00
R / Rfree (%) 17.1 / 19

Other elements in 3iu7:

The structure of M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02 also contains other interesting chemical elements:

Chlorine (Cl) 3 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02 (pdb code 3iu7). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02, PDB code: 3iu7:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 3iu7

Go back to Manganese Binding Sites List in 3iu7
Manganese binding site 1 out of 2 in the M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn286

b:6.8
occ:1.00
OD2 A:ASP142 2.1 7.0 1.0
OXT A:FCD288 2.1 7.8 1.0
OD1 A:ASP131 2.2 7.8 1.0
OE2 A:GLU269 2.2 7.4 1.0
O A:HOH539 2.3 8.0 1.0
OD2 A:ASP131 2.3 7.7 1.0
CG A:ASP131 2.6 7.4 1.0
CG A:ASP142 3.1 5.8 1.0
CD A:GLU269 3.1 5.9 1.0
C A:FCD288 3.2 8.3 1.0
OE1 A:GLU269 3.3 6.9 1.0
OD1 A:ASP142 3.3 6.2 1.0
MN A:MN287 3.5 6.7 1.0
CB A:FCD288 3.8 10.6 1.0
CA A:FCD288 3.8 9.8 1.0
OG1 A:THR133 3.9 7.3 1.0
CB A:ASP131 4.1 6.6 1.0
OB A:FCD288 4.2 9.8 1.0
ND2 A:ASN144 4.2 6.2 1.0
O A:HOH331 4.2 10.6 1.0
OE1 A:GLU238 4.4 11.2 1.0
CB A:ASP142 4.4 6.4 1.0
CG A:GLU269 4.4 6.5 1.0
N A:THR143 4.5 5.1 1.0
O A:THR143 4.6 6.7 1.0
O A:HOH351 4.6 8.0 1.0
C A:ASP142 4.7 5.0 1.0
CB A:ASN144 4.7 6.6 1.0
C A:THR143 4.8 5.9 1.0
CA A:ASP131 4.8 5.9 1.0
O A:HOH410 4.8 11.8 1.0
CA A:ASP142 4.8 4.8 1.0
O A:VAL132 4.8 7.5 1.0
C A:ASP131 4.9 5.3 1.0
N A:VAL132 4.9 6.5 1.0

Manganese binding site 2 out of 2 in 3iu7

Go back to Manganese Binding Sites List in 3iu7
Manganese binding site 2 out of 2 in the M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn287

b:6.7
occ:1.00
OE1 A:GLU269 2.2 6.9 1.0
OE2 A:GLU238 2.2 6.6 1.0
NE2 A:HIS205 2.2 6.4 1.0
OD1 A:ASP142 2.2 6.2 1.0
OXT A:FCD288 2.2 7.8 1.0
OB A:FCD288 2.4 9.8 1.0
C A:FCD288 2.7 8.3 1.0
CD A:GLU238 3.0 7.1 1.0
CD2 A:HIS205 3.1 5.8 1.0
OE1 A:GLU238 3.1 11.2 1.0
CG A:ASP142 3.2 5.8 1.0
CD A:GLU269 3.2 5.9 1.0
CE1 A:HIS205 3.2 5.9 1.0
MN A:MN286 3.5 6.8 1.0
OD2 A:ASP142 3.6 7.0 1.0
OE2 A:GLU269 3.6 7.4 1.0
OG1 A:THR236 3.9 6.1 1.0
CG2 A:THR236 3.9 7.3 1.0
CA A:FCD288 4.1 9.8 1.0
CB A:THR236 4.2 5.8 1.0
CG A:HIS205 4.3 5.2 1.0
CB A:ASP142 4.3 6.4 1.0
ND1 A:HIS205 4.4 6.1 1.0
CG A:GLU238 4.4 7.3 1.0
CG A:GLU269 4.4 6.5 1.0
NE2 A:HIS212 4.5 9.8 1.0
O A:HOH410 4.6 11.8 1.0
CE1 A:PHE211 4.7 7.8 1.0
O A:HOH539 4.7 8.0 1.0
CD2 A:HIS212 5.0 7.7 1.0
OA A:FCD288 5.0 8.6 1.0
O A:HOH503 5.0 26.9 1.0
CB A:GLU238 5.0 6.9 1.0

Reference:

J.P.Lu, S.C.Chai, Q.Z.Ye. Catalysis and Inhibition of Mycobacterium Tuberculosis Methionine Aminopeptidase J.Med.Chem. V. 53 1329 2010.
ISSN: ISSN 0022-2623
PubMed: 20038112
DOI: 10.1021/JM901624N
Page generated: Tue Dec 15 04:11:04 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy