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Manganese in PDB 2evc: Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid

Enzymatic activity of Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid

All present enzymatic activity of Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid:
3.4.11.18;

Protein crystallography data

The structure of Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid, PDB code: 2evc was solved by W.-J.Huang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 37.800, 60.200, 50.400, 90.00, 104.50, 90.00
R / Rfree (%) 21 / 22.9

Other elements in 2evc:

The structure of Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid also contains other interesting chemical elements:

Fluorine (F) 3 atoms
Sodium (Na) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid (pdb code 2evc). 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 E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid, PDB code: 2evc:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 2evc

Go back to Manganese Binding Sites List in 2evc
Manganese binding site 1 out of 2 in the Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)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 E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn901

b:9.1
occ:1.00
 OXT A:FC3999 2.1 11.2 1.0
OD1 A:ASP97 2.1 9.5 1.0
OD1 A:ASP108 2.2 11.9 1.0
OE1 A:GLU235 2.2 8.8 1.0
O A:HOH1010 2.2 11.5 1.0
OD2 A:ASP97 2.4 9.7 1.0
CG A:ASP97 2.6 9.2 1.0
CG A:ASP108 3.1 9.2 1.0
CD A:GLU235 3.1 6.6 1.0
C A:FC3999 3.1 12.2 1.0
OE2 A:GLU235 3.4 7.6 1.0
OD2 A:ASP108 3.4 6.8 1.0
MN A:MN902 3.5 10.6 1.0
O A:HOH1003 3.8 9.7 1.0
CB A:FC3999 3.8 14.4 1.0
OG1 A:THR99 3.8 12.4 1.0
CA A:FC3999 3.8 14.2 1.0
CB A:ASP97 4.1 7.5 1.0
OB A:FC3999 4.1 13.5 1.0
O A:VAL98 4.2 10.0 1.0
OE1 A:GLU204 4.2 17.2 1.0
N A:THR109 4.3 9.5 1.0
O A:HOH1021 4.4 13.3 1.0
CB A:ASP108 4.5 10.4 1.0
CG A:GLU235 4.5 7.2 1.0
O A:HOH1000 4.6 10.6 1.0
O A:THR109 4.6 8.9 1.0
C A:ASP108 4.7 8.8 1.0
C A:THR109 4.7 8.1 1.0
N A:VAL98 4.7 9.3 1.0
O A:HOH1011 4.8 14.6 1.0
CA A:ASP97 4.8 8.4 1.0
CA A:ASP108 4.8 9.0 1.0
C A:ASP97 4.8 9.1 1.0
C A:VAL98 4.8 10.2 1.0
CA A:THR109 4.9 8.1 1.0
CB A:GLU235 4.9 7.3 1.0
CD A:GLU204 4.9 12.7 1.0
CB A:SER110 5.0 7.8 1.0

Manganese binding site 2 out of 2 in 2evc

Go back to Manganese Binding Sites List in 2evc
Manganese binding site 2 out of 2 in the Crystal Structure of E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)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 E. Coli. Methionine Amino Peptidase in Complex with 5-(2-(Trifluoromethyl)Phenyl)Furan-2- Carboxylic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn902

b:10.6
occ:1.00
 OE2 A:GLU204 2.2 11.3 1.0
OE2 A:GLU235 2.2 7.6 1.0
OB A:FC3999 2.2 13.5 1.0
NE2 A:HIS171 2.2 8.8 1.0
OD2 A:ASP108 2.2 6.8 1.0
OXT A:FC3999 2.3 11.2 1.0
C A:FC3999 2.6 12.2 1.0
CD A:GLU204 2.8 12.7 1.0
OE1 A:GLU204 3.0 17.2 1.0
CD2 A:HIS171 3.1 10.2 1.0
CD A:GLU235 3.2 6.6 1.0
CG A:ASP108 3.2 9.2 1.0
CE1 A:HIS171 3.3 8.9 1.0
OE1 A:GLU235 3.5 8.8 1.0
MN A:MN901 3.5 9.1 1.0
OD1 A:ASP108 3.6 11.9 1.0
OG1 A:THR202 3.7 10.3 1.0
CA A:FC3999 4.0 14.2 1.0
CG2 A:THR202 4.1 10.7 1.0
CB A:THR202 4.2 9.9 1.0
CG A:GLU204 4.2 10.4 1.0
CG A:HIS171 4.3 8.3 1.0
CB A:ASP108 4.3 10.4 1.0
ND1 A:HIS171 4.3 8.0 1.0
CG A:GLU235 4.5 7.2 1.0
NE2 A:HIS178 4.6 19.3 1.0
CE1 A:PHE177 4.6 10.3 1.0
O A:HOH1011 4.6 14.6 1.0
O A:HOH1010 4.7 11.5 1.0
OA A:FC3999 4.9 13.8 1.0
CD2 A:HIS178 4.9 20.0 1.0
CB A:GLU204 4.9 8.6 1.0

Reference:

S.X.Xie, W.J.Huang, Z.Q.Ma, M.Huang, R.P.Hanzlik, Q.Z.Ye. Structural Analysis of Metalloform-Selective Inhibition of Methionine Aminopeptidase. Acta Crystallogr.,Sect.D V. 62 425 2006.
ISSN: ISSN 0907-4449
PubMed: 16552144
DOI: 10.1107/S0907444906003878
Page generated: Sat Oct 5 14:00:22 2024

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