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Manganese in PDB 2q94: E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04

Enzymatic activity of E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04

All present enzymatic activity of E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04:
3.4.11.18;

Protein crystallography data

The structure of E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04, PDB code: 2q94 was solved by Q.-Z.Ye, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.91 / 1.63
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 38.199, 60.605, 50.624, 90.00, 104.80, 90.00
R / Rfree (%) 21.3 / 23.8

Other elements in 2q94:

The structure of E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04 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 E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04 (pdb code 2q94). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04, PDB code: 2q94:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 2q94

Go back to Manganese Binding Sites List in 2q94
Manganese binding site 1 out of 2 in the E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn301

b:11.6
occ:1.00
OAQ A:A04400 2.1 13.7 1.0
OD1 A:ASP108 2.2 10.2 1.0
OD1 A:ASP97 2.2 12.2 1.0
OE1 A:GLU235 2.2 9.8 1.0
O A:HOH508 2.2 12.9 1.0
OD2 A:ASP97 2.4 11.2 1.0
CG A:ASP97 2.6 11.2 1.0
CG A:ASP108 3.1 11.3 1.0
CD A:GLU235 3.1 7.6 1.0
CAB A:A04400 3.2 14.0 1.0
OD2 A:ASP108 3.3 11.2 1.0
OE2 A:GLU235 3.3 8.7 1.0
MN A:MN302 3.5 12.2 1.0
O A:HOH503 3.8 10.9 1.0
OG1 A:THR99 3.9 14.5 1.0
CAA A:A04400 4.0 16.9 1.0
CAD A:A04400 4.0 17.3 1.0
CB A:ASP97 4.1 9.7 1.0
OAR A:A04400 4.1 11.6 1.0
O A:VAL98 4.2 11.5 1.0
OE1 A:GLU204 4.3 19.9 1.0
N A:THR109 4.4 10.4 1.0
O A:HOH509 4.4 12.7 1.0
CG A:GLU235 4.5 9.1 1.0
CB A:ASP108 4.5 11.8 1.0
O A:THR109 4.6 9.9 1.0
O A:HOH514 4.6 14.4 1.0
C A:ASP108 4.7 10.9 1.0
C A:THR109 4.7 10.0 1.0
O A:HOH518 4.8 18.9 1.0
N A:VAL98 4.8 11.1 1.0
CA A:ASP108 4.9 11.4 1.0
CA A:ASP97 4.9 9.6 1.0
CA A:THR109 4.9 11.1 1.0
C A:VAL98 4.9 11.2 1.0
CB A:GLU235 4.9 8.8 1.0
C A:ASP97 4.9 10.8 1.0

Manganese binding site 2 out of 2 in 2q94

Go back to Manganese Binding Sites List in 2q94
Manganese binding site 2 out of 2 in the E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A04 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn302

b:12.2
occ:1.00
OE2 A:GLU235 2.1 8.7 1.0
OD2 A:ASP108 2.2 11.2 1.0
OE2 A:GLU204 2.3 12.7 1.0
NE2 A:HIS171 2.3 12.6 1.0
OAR A:A04400 2.3 11.6 1.0
OAQ A:A04400 2.4 13.7 1.0
CAB A:A04400 2.6 14.0 1.0
CD A:GLU204 2.9 16.6 1.0
OE1 A:GLU204 3.0 19.9 1.0
CD A:GLU235 3.2 7.6 1.0
CD2 A:HIS171 3.2 14.0 1.0
CG A:ASP108 3.2 11.3 1.0
CE1 A:HIS171 3.3 14.5 1.0
MN A:MN301 3.5 11.6 1.0
OE1 A:GLU235 3.5 9.8 1.0
OD1 A:ASP108 3.7 10.2 1.0
OG1 A:THR202 3.8 14.1 1.0
CAA A:A04400 4.2 16.9 1.0
CG2 A:THR202 4.2 14.2 1.0
CB A:THR202 4.3 12.5 1.0
CG A:GLU204 4.3 12.9 1.0
CG A:HIS171 4.3 11.1 1.0
CB A:ASP108 4.4 11.8 1.0
ND1 A:HIS171 4.4 11.4 1.0
CG A:GLU235 4.5 9.1 1.0
NE2 A:HIS178 4.5 16.7 1.0
CE1 A:PHE177 4.6 14.3 1.0
O A:HOH508 4.7 12.9 1.0
O A:HOH518 4.8 18.9 1.0
CD2 A:HIS178 4.9 18.1 1.0
OAP A:A04400 5.0 14.7 1.0

Reference:

Z.Q.Ma, S.X.Xie, Q.Q.Huang, F.J.Nan, T.D.Hurley, Q.Z.Ye. Structural Analysis of Inhibition of E. Coli Methionine Aminopeptidase: Implication of Loop Flexibility in Selective Inhibition of Bacterial Enzymes. Bmc Struct.Biol. V. 7 84 2007.
ISSN: ESSN 1472-6807
PubMed: 18093325
DOI: 10.1186/1472-6807-7-84
Page generated: Sat Oct 5 14:58:28 2024

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