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Manganese in PDB 1n51: Aminopeptidase P in Complex with the Inhibitor Apstatin

Enzymatic activity of Aminopeptidase P in Complex with the Inhibitor Apstatin

All present enzymatic activity of Aminopeptidase P in Complex with the Inhibitor Apstatin:
3.4.11.9;

Protein crystallography data

The structure of Aminopeptidase P in Complex with the Inhibitor Apstatin, PDB code: 1n51 was solved by S.C.Graham, M.J.Maher, M.H.Lee, W.H.Simmons, H.C.Freeman, J.M.Guss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.90 / 2.30
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 139.319, 139.319, 231.005, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / 20.4

Manganese Binding Sites:

The binding sites of Manganese atom in the Aminopeptidase P in Complex with the Inhibitor Apstatin (pdb code 1n51). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Aminopeptidase P in Complex with the Inhibitor Apstatin, PDB code: 1n51:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in 1n51

Go back to Manganese Binding Sites List in 1n51
Manganese binding site 1 out of 3 in the Aminopeptidase P in Complex with the Inhibitor Apstatin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Aminopeptidase P in Complex with the Inhibitor Apstatin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn2001

b:34.4
occ:1.00
OE2 A:GLU406 2.0 31.1 1.0
NE2 A:HIS354 2.1 36.6 1.0
OD2 A:ASP271 2.1 32.4 1.0
O2 B:01B1 2.2 68.8 1.0
OE2 A:GLU383 2.3 40.2 1.0
CD A:GLU406 3.0 37.5 1.0
CD2 A:HIS354 3.0 29.3 1.0
CE1 A:HIS354 3.1 33.6 1.0
CG A:ASP271 3.1 33.3 1.0
CD A:GLU383 3.1 39.4 1.0
MN A:MN2002 3.3 35.7 1.0
OE1 A:GLU383 3.3 40.7 1.0
C2 B:01B1 3.4 76.2 1.0
OE1 A:GLU406 3.5 33.3 1.0
OD1 A:ASP271 3.5 34.5 1.0
CG2 A:THR381 3.6 32.0 1.0
O3 B:01B1 3.6 81.2 1.0
OG1 A:THR381 3.6 32.5 1.0
C3 B:01B1 3.7 80.3 1.0
CB A:THR381 3.9 34.6 1.0
C1 B:01B1 4.1 75.4 1.0
ND1 A:HIS354 4.2 28.9 1.0
CG A:HIS354 4.2 32.4 1.0
CB A:ASP271 4.3 30.7 1.0
CG A:GLU406 4.4 35.9 1.0
N2 B:01B1 4.4 71.1 1.0
CG A:GLU383 4.4 36.0 1.0
N B:PRO2 4.7 83.3 1.0
CG2 A:VAL360 4.9 33.1 1.0

Manganese binding site 2 out of 3 in 1n51

Go back to Manganese Binding Sites List in 1n51
Manganese binding site 2 out of 3 in the Aminopeptidase P in Complex with the Inhibitor Apstatin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Aminopeptidase P in Complex with the Inhibitor Apstatin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn2002

b:35.7
occ:1.00
O2 B:01B1 1.9 68.8 1.0
OD1 A:ASP271 2.1 34.5 1.0
OE1 A:GLU406 2.1 33.3 1.0
OD1 A:ASP260 2.2 28.0 1.0
OD2 A:ASP260 2.5 29.8 1.0
N2 B:01B1 2.6 71.1 1.0
CG A:ASP260 2.6 29.5 1.0
C2 B:01B1 2.7 76.2 1.0
CG A:ASP271 3.0 33.3 1.0
CD A:GLU406 3.0 37.5 1.0
OD2 A:ASP271 3.2 32.4 1.0
C1 B:01B1 3.2 75.4 1.0
OE2 A:GLU406 3.2 31.1 1.0
MN A:MN2001 3.3 34.4 1.0
OG1 A:THR273 3.5 34.9 1.0
OH A:TYR229 3.7 31.9 1.0
C3 B:01B1 4.1 80.3 1.0
CZ A:TYR229 4.1 32.8 1.0
OE1 A:GLU383 4.1 40.7 1.0
CB A:ASP260 4.2 29.0 1.0
CB A:ASP271 4.4 30.7 1.0
CG A:GLU406 4.4 35.9 1.0
C6 B:01B1 4.4 75.0 1.0
CE2 A:TYR229 4.5 27.9 1.0
C A:ASP271 4.6 33.9 1.0
O A:ILE272 4.7 35.2 1.0
N A:ILE272 4.8 33.4 1.0
O A:ASP271 4.8 37.4 1.0
CA A:ASP271 4.8 33.3 1.0
NE A:ARG404 4.8 31.3 1.0
CD A:GLU383 4.8 39.4 1.0
O3 B:01B1 4.8 81.2 1.0
C A:ILE272 4.8 36.9 1.0
CE1 A:TYR229 4.8 28.3 1.0
OE2 A:GLU383 4.8 40.2 1.0
CD B:PRO2 4.9 80.8 1.0
N B:PRO2 4.9 83.3 1.0
CA A:ASP260 4.9 32.3 1.0
CB A:THR273 4.9 35.8 1.0
CB A:GLU406 5.0 34.8 1.0

Manganese binding site 3 out of 3 in 1n51

Go back to Manganese Binding Sites List in 1n51
Manganese binding site 3 out of 3 in the Aminopeptidase P in Complex with the Inhibitor Apstatin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Aminopeptidase P in Complex with the Inhibitor Apstatin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn2003

b:45.9
occ:1.00
O A:HOH2174 2.0 31.6 1.0
O A:HOH2173 2.1 38.0 1.0
O A:HOH2166 2.2 45.4 1.0
O A:HOH2172 2.3 36.2 1.0
O A:HOH2171 2.3 45.6 1.0
O A:HOH2195 3.8 51.8 1.0
O A:ARG399 4.0 34.3 0.5
O A:ARG399 4.0 34.2 0.5
OE2 A:GLU396 4.2 36.4 1.0
O A:GLN397 4.6 37.1 1.0
O A:HOH2031 4.6 41.0 1.0
O A:GLU396 4.7 35.2 1.0
O A:HOH2196 5.0 61.4 1.0

Reference:

S.C.Graham, M.J.Maher, W.H.Simmons, H.C.Freeman, J.M.Guss. Structure of Escherichia Coli Aminopeptidase P in Complex with the Inhibitor Apstatin. Acta Crystallogr.,Sect.D V. 60 1770 2004.
ISSN: ISSN 0907-4449
PubMed: 15388923
DOI: 10.1107/S0907444904018724
Page generated: Sat Oct 5 11:50:08 2024

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