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Manganese in PDB 1xnz: Crystal Structure of Mn(II) Form of E. Coli. Methionine Aminopeptidase in Complex with 5-(2-Chlorophenyl)Furan-2- Carboxylic Acid

Enzymatic activity of Crystal Structure of Mn(II) Form of E. Coli. Methionine Aminopeptidase in Complex with 5-(2-Chlorophenyl)Furan-2- Carboxylic Acid

All present enzymatic activity of Crystal Structure of Mn(II) Form of E. Coli. Methionine Aminopeptidase in Complex with 5-(2-Chlorophenyl)Furan-2- Carboxylic Acid:
3.4.11.18;

Protein crystallography data

The structure of Crystal Structure of Mn(II) Form of E. Coli. Methionine Aminopeptidase in Complex with 5-(2-Chlorophenyl)Furan-2- Carboxylic Acid, PDB code: 1xnz was solved by Q.-Z.Ye, S.-X.Xie, M.Huang, W.-J.Huang, J.-P.Lu, Z.-Q.Ma, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.52
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 37.600, 60.300, 49.700, 90.00, 104.80, 90.00
R / Rfree (%) 21.9 / 25

Other elements in 1xnz:

The structure of Crystal Structure of Mn(II) Form of E. Coli. Methionine Aminopeptidase in Complex with 5-(2-Chlorophenyl)Furan-2- Carboxylic Acid also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Sodium (Na) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Mn(II) Form of E. Coli. Methionine Aminopeptidase in Complex with 5-(2-Chlorophenyl)Furan-2- Carboxylic Acid (pdb code 1xnz). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Mn(II) Form of E. Coli. Methionine Aminopeptidase in Complex with 5-(2-Chlorophenyl)Furan-2- Carboxylic Acid, PDB code: 1xnz:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1xnz

Go back to Manganese Binding Sites List in 1xnz
Manganese binding site 1 out of 2 in the Crystal Structure of Mn(II) Form of E. Coli. Methionine Aminopeptidase in Complex with 5-(2-Chlorophenyl)Furan-2- Carboxylic Acid


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Mn(II) Form of E. Coli. Methionine Aminopeptidase in Complex with 5-(2-Chlorophenyl)Furan-2- Carboxylic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn265

b:9.4
occ:1.00
 OXT A:FCD268 2.0 7.7 1.0
OE1 A:GLU235 2.2 9.0 1.0
OD1 A:ASP108 2.2 10.6 1.0
OD1 A:ASP97 2.2 9.8 1.0
O A:HOH411 2.2 8.7 1.0
OD2 A:ASP97 2.4 12.4 1.0
CG A:ASP97 2.6 9.8 1.0
CG A:ASP108 3.0 9.3 1.0
CD A:GLU235 3.1 6.3 1.0
C A:FCD268 3.1 11.8 1.0
OD2 A:ASP108 3.2 7.2 1.0
OE2 A:GLU235 3.4 9.1 1.0
MN A:MN266 3.5 9.3 1.0
O A:HOH271 3.7 8.2 1.0
CA A:FCD268 3.8 12.6 1.0
CB A:FCD268 3.8 13.3 1.0
OG1 A:THR99 3.8 11.2 1.0
CB A:ASP97 4.1 6.9 1.0
OB A:FCD268 4.1 12.0 1.0
OE1 A:GLU204 4.2 17.2 1.0
O A:VAL98 4.3 7.2 1.0
N A:THR109 4.3 7.1 1.0
O A:HOH282 4.4 14.0 1.0
CB A:ASP108 4.4 9.5 1.0
CG A:GLU235 4.4 8.6 1.0
O A:HOH277 4.5 9.5 1.0
O A:THR109 4.6 8.6 1.0
C A:ASP108 4.7 7.6 1.0
C A:THR109 4.7 7.9 1.0
O A:HOH291 4.7 15.2 1.0
N A:VAL98 4.8 9.6 1.0
CA A:ASP97 4.8 8.2 1.0
CA A:ASP108 4.8 8.4 1.0
CB A:GLU235 4.9 7.0 1.0
CA A:THR109 4.9 7.5 1.0
CD A:GLU204 4.9 11.7 1.0
C A:ASP97 4.9 8.6 1.0
C A:VAL98 4.9 8.6 1.0
CB A:SER110 4.9 9.1 1.0

Manganese binding site 2 out of 2 in 1xnz

Go back to Manganese Binding Sites List in 1xnz
Manganese binding site 2 out of 2 in the Crystal Structure of Mn(II) Form of E. Coli. Methionine Aminopeptidase in Complex with 5-(2-Chlorophenyl)Furan-2- Carboxylic Acid


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Mn(II) Form of E. Coli. Methionine Aminopeptidase in Complex with 5-(2-Chlorophenyl)Furan-2- Carboxylic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn266

b:9.3
occ:1.00
 OE2 A:GLU235 2.1 9.1 1.0
NE2 A:HIS171 2.1 9.4 1.0
OD2 A:ASP108 2.2 7.2 1.0
OE2 A:GLU204 2.2 10.0 1.0
OB A:FCD268 2.2 12.0 1.0
OXT A:FCD268 2.3 7.7 1.0
C A:FCD268 2.6 11.8 1.0
CD A:GLU204 2.9 11.7 1.0
OE1 A:GLU204 3.0 17.2 1.0
CD2 A:HIS171 3.0 9.2 1.0
CD A:GLU235 3.1 6.3 1.0
CG A:ASP108 3.2 9.3 1.0
CE1 A:HIS171 3.2 9.1 1.0
OE1 A:GLU235 3.5 9.0 1.0
MN A:MN265 3.5 9.4 1.0
OD1 A:ASP108 3.7 10.6 1.0
OG1 A:THR202 3.7 9.0 1.0
CA A:FCD268 4.0 12.6 1.0
CG2 A:THR202 4.1 8.7 1.0
CG A:HIS171 4.2 7.5 1.0
CB A:THR202 4.2 8.8 1.0
ND1 A:HIS171 4.3 8.3 1.0
CG A:GLU204 4.3 11.8 1.0
CB A:ASP108 4.3 9.5 1.0
CG A:GLU235 4.4 8.6 1.0
NE2 A:HIS178 4.5 23.3 1.0
CE1 A:PHE177 4.6 12.4 1.0
O A:HOH291 4.6 15.2 1.0
O A:HOH411 4.7 8.7 1.0
OA A:FCD268 4.9 13.4 1.0
CB A:GLU204 4.9 9.4 1.0

Reference:

Q.-Z.Ye, S.-X.Xie, M.Huang, W.-J.Huang, J.-P.Lu, Z.-Q.Ma. Metalloform-Selective Inhibitors of Escherichia Coli Methionine Aminopeptidase and X-Ray Structure of A Mn(II)-Form Enzyme Complexed with An Inhibitor. J.Am.Chem.Soc. V. 126 13940 2004.
ISSN: ISSN 0002-7863
PubMed: 15506752
DOI: 10.1021/JA045864P
Page generated: Sat Oct 5 13:08:10 2024

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