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Manganese in PDB 1a16: Aminopeptidase P From E. Coli with the Inhibitor Pro-Leu

Enzymatic activity of Aminopeptidase P From E. Coli with the Inhibitor Pro-Leu

All present enzymatic activity of Aminopeptidase P From E. Coli with the Inhibitor Pro-Leu:
3.4.11.9;

Protein crystallography data

The structure of Aminopeptidase P From E. Coli with the Inhibitor Pro-Leu, PDB code: 1a16 was solved by M.C.Wilce, C.S.Bond, P.E.Lilley, N.E.Dixon, 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) 50.00 / 2.30
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 177.300, 177.300, 96.500, 90.00, 90.00, 120.00
R / Rfree (%) 18.4 / 22.6

Manganese Binding Sites:

The binding sites of Manganese atom in the Aminopeptidase P From E. Coli with the Inhibitor Pro-Leu (pdb code 1a16). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Aminopeptidase P From E. Coli with the Inhibitor Pro-Leu, PDB code: 1a16:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1a16

Go back to Manganese Binding Sites List in 1a16
Manganese binding site 1 out of 2 in the Aminopeptidase P From E. Coli with the Inhibitor Pro-Leu


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Aminopeptidase P From E. Coli with the Inhibitor Pro-Leu within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn443

b:24.2
occ:1.00
OE2 A:GLU406 2.0 17.1 1.0
OE2 A:GLU383 2.1 20.2 1.0
NE2 A:HIS354 2.1 12.1 1.0
O A:HOH790 2.1 26.3 1.0
OD2 A:ASP271 2.1 13.7 1.0
CD A:GLU383 3.1 23.3 1.0
CD2 A:HIS354 3.2 8.0 1.0
CG A:ASP271 3.2 16.6 1.0
CE1 A:HIS354 3.2 10.1 1.0
CD A:GLU406 3.3 21.1 1.0
MN A:MN444 3.3 23.9 1.0
OE1 A:GLU383 3.4 26.7 1.0
OD1 A:ASP271 3.5 17.2 1.0
OE1 A:GLU406 3.7 21.7 1.0
O A:HOH786 3.8 40.4 1.0
OG1 A:THR381 3.8 16.4 1.0
CG2 A:THR381 3.9 8.9 1.0
O A:HOH473 3.9 27.3 1.0
N A:PRO441 4.1 38.7 1.0
CB A:THR381 4.1 13.1 1.0
CG A:HIS354 4.2 10.7 1.0
ND1 A:HIS354 4.2 10.5 1.0
CG A:GLU383 4.4 18.2 1.0
CA A:PRO441 4.5 41.1 1.0
CG A:GLU406 4.5 20.9 1.0
CB A:ASP271 4.6 15.0 1.0
NE2 A:HIS361 4.8 23.9 1.0
O A:HOH788 4.8 26.9 1.0
CD2 A:HIS361 5.0 26.2 1.0
CD A:PRO441 5.0 33.0 1.0

Manganese binding site 2 out of 2 in 1a16

Go back to Manganese Binding Sites List in 1a16
Manganese binding site 2 out of 2 in the Aminopeptidase P From E. Coli with the Inhibitor Pro-Leu


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Aminopeptidase P From E. Coli with the Inhibitor Pro-Leu within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn444

b:23.9
occ:1.00
OD1 A:ASP271 2.0 17.2 1.0
O A:HOH790 2.1 26.3 1.0
OE1 A:GLU406 2.2 21.7 1.0
OD1 A:ASP260 2.3 19.4 1.0
OD2 A:ASP260 2.3 20.8 1.0
O A:HOH473 2.4 27.3 1.0
CG A:ASP260 2.8 18.6 1.0
CG A:ASP271 3.1 16.6 1.0
CD A:GLU406 3.1 21.1 1.0
OE2 A:GLU406 3.2 17.1 1.0
MN A:MN443 3.3 24.2 1.0
OD2 A:ASP271 3.3 13.7 1.0
OG1 A:THR273 3.5 19.4 1.0
OH A:TYR229 3.6 17.4 1.0
OE1 A:GLU383 4.1 26.7 1.0
CZ A:TYR229 4.1 17.8 1.0
O A:HOH786 4.1 40.4 1.0
CB A:ASP260 4.2 15.8 1.0
CE2 A:TYR229 4.3 22.2 1.0
CG A:GLU406 4.4 20.9 1.0
N A:PRO441 4.5 38.7 1.0
CD A:PRO441 4.5 33.0 1.0
OE2 A:GLU383 4.5 20.2 1.0
CB A:ASP271 4.5 15.0 1.0
O A:ASP271 4.6 19.4 1.0
O A:ILE272 4.7 23.8 1.0
C A:ASP271 4.7 16.6 1.0
N A:ILE272 4.7 15.8 1.0
NE A:ARG404 4.8 24.6 1.0
C A:ILE272 4.8 20.0 1.0
CA A:ASP260 4.8 17.1 1.0
CE1 A:TYR229 4.8 19.3 1.0
CD A:GLU383 4.9 23.3 1.0
CB A:THR273 4.9 14.2 1.0
CB A:GLU406 4.9 16.7 1.0
CA A:ASP271 4.9 14.6 1.0

Reference:

M.C.Wilce, C.S.Bond, N.E.Dixon, H.C.Freeman, J.M.Guss, P.E.Lilley, J.A.Wilce. Structure and Mechanism of A Proline-Specific Aminopeptidase From Escherichia Coli. Proc.Natl.Acad.Sci.Usa V. 95 3472 1998.
ISSN: ISSN 0027-8424
PubMed: 9520390
DOI: 10.1073/PNAS.95.7.3472
Page generated: Tue Dec 15 03:46:01 2020

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