Atomistry » Manganese » PDB 3g0z-3hvq » 3h8f
Atomistry »
  Manganese »
    PDB 3g0z-3hvq »
      3h8f »

Manganese in PDB 3h8f: High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida

Enzymatic activity of High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida

All present enzymatic activity of High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida:
3.4.11.1;

Protein crystallography data

The structure of High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida, PDB code: 3h8f was solved by A.Kale, B.W.Dijkstra, T.Sonke, A.M.W.H.Thunnissen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.45 / 2.20
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 95.786, 95.931, 96.308, 68.43, 76.31, 94.86
R / Rfree (%) 19.2 / 25.1

Other elements in 3h8f:

The structure of High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida also contains other interesting chemical elements:

Potassium (K) 6 atoms
Zinc (Zn) 6 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida (pdb code 3h8f). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 6 binding sites of Manganese where determined in the High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida, PDB code: 3h8f:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6;

Manganese binding site 1 out of 6 in 3h8f

Go back to Manganese Binding Sites List in 3h8f
Manganese binding site 1 out of 6 in the High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn502

b:38.0
occ:1.00
 OD1 A:ASP349 2.1 8.8 1.0
O A:ASP349 2.1 5.8 1.0
OE2 A:GLU351 2.3 9.6 1.0
O A:HOH3681 2.3 14.2 1.0
OD2 A:ASP272 2.4 8.8 1.0
C A:ASP349 3.0 7.0 1.0
CG A:ASP349 3.1 7.5 1.0
CD A:GLU351 3.2 7.1 1.0
CG A:ASP272 3.3 6.0 1.0
ZN A:ZN501 3.3 20.0 1.0
CA A:ASP349 3.4 7.0 1.0
OE1 A:GLU351 3.4 6.0 1.0
OD1 A:ASP272 3.5 5.4 1.0
CB A:ASP349 3.8 5.6 1.0
NZ A:LYS279 3.8 6.7 1.0
OD2 A:ASP349 3.9 7.8 1.0
O A:HOH2219 4.1 26.4 1.0
N A:ALA350 4.2 7.4 1.0
CE A:LYS279 4.2 5.2 1.0
N A:GLU351 4.3 6.1 1.0
O1 A:BCT504 4.3 10.1 1.0
CG A:GLU351 4.6 6.2 1.0
CA A:ALA350 4.6 7.2 1.0
CB A:ASP272 4.7 5.3 1.0
CA A:GLY274 4.7 2.0 1.0
N A:ASP349 4.8 6.2 1.0
OD2 A:ASP290 4.8 10.8 1.0
ND2 A:ASN322 4.9 6.6 1.0
O A:THR348 4.9 7.0 1.0

Manganese binding site 2 out of 6 in 3h8f

Go back to Manganese Binding Sites List in 3h8f
Manganese binding site 2 out of 6 in the High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn502

b:34.8
occ:1.00
 OE2 B:GLU351 2.2 7.0 1.0
O B:HOH3682 2.3 10.4 1.0
O B:ASP349 2.3 5.8 1.0
OD1 B:ASP349 2.3 6.5 1.0
OD2 B:ASP272 2.3 7.1 1.0
C B:ASP349 3.1 6.2 1.0
CG B:ASP272 3.1 5.7 1.0
CD B:GLU351 3.2 5.1 1.0
ZN B:ZN501 3.2 21.2 1.0
OD1 B:ASP272 3.2 2.9 1.0
CG B:ASP349 3.2 7.4 1.0
OE1 B:GLU351 3.4 3.4 1.0
CA B:ASP349 3.5 5.6 1.0
CB B:ASP349 3.9 5.5 1.0
NZ B:LYS279 4.1 7.8 1.0
OD2 B:ASP349 4.1 12.8 1.0
O1 B:BCT504 4.1 12.7 1.0
CE B:LYS279 4.2 2.9 1.0
N B:ALA350 4.2 6.7 1.0
N B:GLU351 4.3 6.2 1.0
CG B:GLU351 4.6 5.7 1.0
CB B:ASP272 4.6 4.3 1.0
CA B:ALA350 4.6 6.6 1.0
ND2 B:ASN322 4.6 2.0 1.0
OD2 B:ASP290 4.7 12.8 1.0
N B:ASP349 4.9 5.2 1.0
CA B:GLY274 4.9 4.2 1.0
CB B:GLU351 5.0 5.6 1.0

Manganese binding site 3 out of 6 in 3h8f

Go back to Manganese Binding Sites List in 3h8f
Manganese binding site 3 out of 6 in the High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn502

b:34.4
occ:1.00
 O C:ASP349 2.1 2.8 1.0
O C:HOH3683 2.1 14.6 1.0
OE2 C:GLU351 2.2 7.1 1.0
OD2 C:ASP272 2.3 3.4 1.0
OD1 C:ASP349 2.3 6.3 1.0
C C:ASP349 3.0 2.2 1.0
ZN C:ZN501 3.0 17.3 1.0
CD C:GLU351 3.1 6.6 1.0
CG C:ASP272 3.3 4.1 1.0
CG C:ASP349 3.3 4.9 1.0
OE1 C:GLU351 3.3 7.0 1.0
CA C:ASP349 3.5 2.2 1.0
OD1 C:ASP272 3.5 5.5 1.0
O3 C:BCT504 3.8 9.5 1.0
CB C:ASP349 3.9 2.8 1.0
NZ C:LYS279 4.1 4.2 1.0
N C:ALA350 4.1 2.4 1.0
N C:GLU351 4.1 2.2 1.0
OD2 C:ASP349 4.2 5.9 1.0
CE C:LYS279 4.4 4.1 1.0
CA C:ALA350 4.5 2.5 1.0
O C:HOH3790 4.5 15.2 1.0
CG C:GLU351 4.5 4.5 1.0
CB C:ASP272 4.6 2.0 1.0
OD2 C:ASP290 4.6 8.4 1.0
C C:BCT504 4.7 9.1 1.0
C C:ALA350 4.9 2.2 1.0
N C:ASP349 4.9 2.0 1.0
NZ C:LYS267 4.9 6.0 1.0
ND2 C:ASN322 4.9 2.0 1.0
O C:THR348 5.0 2.3 1.0
CB C:GLU351 5.0 2.8 1.0

Manganese binding site 4 out of 6 in 3h8f

Go back to Manganese Binding Sites List in 3h8f
Manganese binding site 4 out of 6 in the High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn502

b:35.4
occ:1.00
 OD1 D:ASP349 2.1 11.3 1.0
OD2 D:ASP272 2.2 7.2 1.0
O D:ASP349 2.3 6.0 1.0
OE2 D:GLU351 2.3 8.1 1.0
O D:HOH3684 2.3 2.0 1.0
CG D:ASP349 3.1 6.9 1.0
ZN D:ZN501 3.1 21.2 1.0
C D:ASP349 3.1 5.8 1.0
CG D:ASP272 3.2 9.2 1.0
CD D:GLU351 3.2 8.4 1.0
OE1 D:GLU351 3.4 9.3 1.0
OD1 D:ASP272 3.5 11.4 1.0
CA D:ASP349 3.5 5.3 1.0
O2 D:BCT504 3.9 13.0 1.0
CB D:ASP349 3.9 5.2 1.0
OD2 D:ASP349 4.0 4.4 1.0
CE D:LYS279 4.1 2.0 1.0
N D:ALA350 4.3 6.0 1.0
NZ D:LYS279 4.4 3.3 1.0
N D:GLU351 4.5 6.5 1.0
CB D:ASP272 4.5 6.7 1.0
OD2 D:ASP290 4.5 11.8 1.0
CG D:GLU351 4.6 6.2 1.0
CA D:ALA350 4.8 6.1 1.0
ND2 D:ASN322 4.8 7.5 1.0
C D:BCT504 4.9 12.9 1.0
N D:ASP349 4.9 4.3 1.0
CA D:GLY274 5.0 4.0 1.0
NZ D:LYS267 5.0 4.5 1.0

Manganese binding site 5 out of 6 in 3h8f

Go back to Manganese Binding Sites List in 3h8f
Manganese binding site 5 out of 6 in the High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mn502

b:33.9
occ:1.00
 OD2 E:ASP272 2.2 4.5 1.0
OD1 E:ASP349 2.2 10.1 1.0
O E:ASP349 2.3 4.9 1.0
OE2 E:GLU351 2.3 8.1 1.0
O E:HOH3685 2.4 2.7 1.0
CG E:ASP272 3.1 3.8 1.0
C E:ASP349 3.1 3.8 1.0
CG E:ASP349 3.2 6.2 1.0
ZN E:ZN501 3.2 18.3 1.0
OD1 E:ASP272 3.2 3.7 1.0
CD E:GLU351 3.2 8.1 1.0
CA E:ASP349 3.5 3.8 1.0
OE1 E:GLU351 3.5 8.5 1.0
CB E:ASP349 3.9 4.3 1.0
NZ E:LYS279 3.9 4.4 1.0
OD2 E:ASP349 4.0 9.9 1.0
O3 E:BCT504 4.2 7.9 1.0
N E:ALA350 4.2 3.5 1.0
N E:GLU351 4.3 4.1 1.0
CE E:LYS279 4.3 2.0 1.0
CB E:ASP272 4.5 3.4 1.0
ND2 E:ASN322 4.6 5.5 1.0
CA E:ALA350 4.6 4.1 1.0
OD2 E:ASP290 4.6 5.1 1.0
CG E:GLU351 4.6 4.8 1.0
N E:ASP349 4.8 4.1 1.0
CA E:GLY274 4.8 2.1 1.0
CB E:GLU351 4.9 3.8 1.0
NZ E:LYS267 5.0 2.0 1.0
C E:ALA350 5.0 3.3 1.0

Manganese binding site 6 out of 6 in 3h8f

Go back to Manganese Binding Sites List in 3h8f
Manganese binding site 6 out of 6 in the High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of High pH Native Structure of Leucine Aminopeptidase From Pseudomonas Putida within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mn502

b:37.8
occ:1.00
 O F:HOH3686 2.1 13.8 1.0
O F:ASP349 2.1 3.9 1.0
OD1 F:ASP349 2.2 7.8 1.0
OE2 F:GLU351 2.4 8.0 1.0
OD2 F:ASP272 2.5 12.3 1.0
C F:ASP349 3.1 4.6 1.0
CG F:ASP349 3.1 6.9 1.0
ZN F:ZN501 3.3 20.6 1.0
CD F:GLU351 3.4 8.1 1.0
CG F:ASP272 3.5 5.4 1.0
CA F:ASP349 3.5 4.7 1.0
OD1 F:ASP272 3.7 5.1 1.0
OE1 F:GLU351 3.7 5.1 1.0
CB F:ASP349 3.8 4.7 1.0
OD2 F:ASP349 3.8 10.1 1.0
NZ F:LYS279 3.9 7.9 1.0
O3 F:BCT504 4.1 12.8 1.0
N F:ALA350 4.2 5.0 1.0
CE F:LYS279 4.2 6.6 1.0
N F:GLU351 4.4 7.2 1.0
CA F:ALA350 4.6 5.9 1.0
CG F:GLU351 4.8 6.4 1.0
CB F:ASP272 4.8 3.2 1.0
OD2 F:ASP290 4.9 7.1 1.0
NZ F:LYS267 4.9 16.1 1.0
N F:ASP349 4.9 4.1 1.0
C F:BCT504 5.0 11.8 1.0

Reference:

A.Kale, T.Pijning, T.Sonke, B.W.Dijkstra, A.M.Thunnissen. Crystal Structure of the Leucine Aminopeptidase From Pseudomonas Putida Reveals the Molecular Basis For Its Enantioselectivity and Broad Substrate Specificity. J.Mol.Biol. V. 398 703 2010.
ISSN: ISSN 0022-2836
PubMed: 20359484
DOI: 10.1016/J.JMB.2010.03.042
Page generated: Tue Dec 15 04:10:20 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy