Atomistry » Manganese » PDB 5nha-5raa » 5oey
Atomistry »
  Manganese »
    PDB 5nha-5raa »
      5oey »

Manganese in PDB 5oey: Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form.

Enzymatic activity of Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form.

All present enzymatic activity of Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form.:
3.1.3.11;

Protein crystallography data

The structure of Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form., PDB code: 5oey was solved by M.Yuan, M.G.Vasquez-Valdivieso, I.W.Mcnae, P.A.M.Michels, L.A.Fothergill-Gilmore, M.D.Walkinshaw, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.14 / 2.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 92.010, 104.150, 137.740, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 24.1

Other elements in 5oey:

The structure of Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form. also contains other interesting chemical elements:

Potassium (K) 4 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form. (pdb code 5oey). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 8 binding sites of Manganese where determined in the Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form., PDB code: 5oey:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Manganese binding site 1 out of 8 in 5oey

Go back to Manganese Binding Sites List in 5oey
Manganese binding site 1 out of 8 in the Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form.


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 Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn702

b:35.3
occ:1.00
 O2 A:PO4701 1.9 34.8 1.0
OE1 A:GLU97 2.2 38.0 1.0
OD1 A:ASP118 2.2 27.3 1.0
O A:LEU120 2.2 26.9 1.0
CG A:ASP118 3.2 23.9 1.0
C A:LEU120 3.2 26.3 1.0
CD A:GLU97 3.2 36.8 1.0
OE2 A:GLU98 3.2 38.9 1.0
P A:PO4701 3.3 36.7 1.0
OD2 A:ASP118 3.4 24.2 1.0
K A:K704 3.5 27.4 1.0
OD1 A:ASP74 3.6 44.7 1.0
O1 A:PO4701 3.7 40.8 1.0
CG A:GLU97 3.7 36.3 1.0
N A:ASP121 4.0 28.6 1.0
N A:LEU120 4.0 24.9 1.0
CA A:ASP121 4.1 30.7 1.0
MN A:MN703 4.1 34.2 1.0
CA A:LEU120 4.1 24.6 1.0
OG A:SER123 4.1 48.8 1.0
O3 A:PO4701 4.2 36.3 1.0
OE2 A:GLU97 4.3 42.2 1.0
O4 A:PO4701 4.4 34.5 1.0
CD A:GLU98 4.5 38.4 1.0
CB A:ASP118 4.5 22.5 1.0
CD A:PRO119 4.7 22.3 1.0
CG A:ASP74 4.7 40.5 1.0
CB A:LEU120 4.7 24.6 1.0
CB A:GLU97 4.7 34.5 1.0
C A:ASP118 4.9 21.9 1.0
CA A:ASP118 4.9 22.0 1.0
N A:PRO119 4.9 21.6 1.0

Manganese binding site 2 out of 8 in 5oey

Go back to Manganese Binding Sites List in 5oey
Manganese binding site 2 out of 8 in the Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form.


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 Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn703

b:34.2
occ:1.00
 OE2 A:GLU284 2.2 36.2 1.0
OD1 A:ASP121 2.2 27.1 1.0
OD2 A:ASP118 2.2 24.2 1.0
O3 A:PO4701 2.5 36.3 1.0
O2 A:PO4701 2.6 34.8 1.0
P A:PO4701 2.7 36.7 1.0
O4 A:PO4701 2.8 34.5 1.0
CG A:ASP121 3.2 31.6 1.0
CD A:GLU284 3.3 36.0 1.0
CG A:ASP118 3.3 23.9 1.0
CB A:ASP121 3.5 31.6 1.0
CA A:ASP121 3.7 30.7 1.0
OD1 A:ASP118 3.9 27.3 1.0
CG A:GLU284 3.9 33.5 1.0
OE1 A:GLU97 4.1 38.0 1.0
MN A:MN702 4.1 35.3 1.0
NH2 A:ARG280 4.2 49.1 1.0
O1 A:PO4701 4.2 40.8 1.0
OE1 A:GLU284 4.3 39.8 1.0
OD2 A:ASP121 4.3 31.1 1.0
N A:GLY122 4.4 30.4 1.0
CB A:ASP118 4.4 22.5 1.0
C A:ASP121 4.6 30.3 1.0
N A:ASP121 4.7 28.6 1.0
CD A:GLU97 4.8 36.8 1.0
O A:LEU120 4.8 26.9 1.0
OE2 A:GLU97 5.0 42.2 1.0
CD1 A:ILE135 5.0 15.5 1.0

Manganese binding site 3 out of 8 in 5oey

Go back to Manganese Binding Sites List in 5oey
Manganese binding site 3 out of 8 in the Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn702

b:15.7
occ:1.00
 O B:HOH801 2.1 8.9 1.0
OE1 B:GLU97 2.1 18.9 1.0
O B:LEU120 2.1 21.5 1.0
OD1 B:ASP118 2.2 13.8 1.0
O1 B:PO4701 3.0 45.3 1.0
C B:LEU120 3.1 21.2 1.0
CG B:ASP118 3.1 14.2 1.0
CD B:GLU97 3.1 20.1 1.0
OD2 B:ASP118 3.3 16.3 1.0
O4 B:PO4701 3.4 39.1 1.0
MN B:MN703 3.4 21.0 1.0
OE2 B:GLU98 3.5 36.0 1.0
OE2 B:GLU97 3.6 22.6 1.0
P B:PO4701 3.7 49.3 1.0
OD1 B:ASP74 3.8 27.1 1.0
N B:ASP121 3.8 24.6 1.0
CA B:ASP121 3.8 27.4 1.0
OG B:SER123 4.1 24.9 1.0
N B:LEU120 4.1 17.7 1.0
O2 B:PO4701 4.1 40.9 1.0
CA B:LEU120 4.1 18.9 1.0
CG B:GLU97 4.4 20.1 1.0
CB B:ASP118 4.5 14.1 1.0
CD B:GLU98 4.7 30.9 1.0
CB B:LEU120 4.8 18.7 1.0
CB B:ASP121 4.8 30.4 1.0
C B:ASP121 4.8 26.7 1.0
N B:GLY122 4.8 26.8 1.0
CB B:GLU97 4.8 20.0 1.0
CD B:PRO119 4.9 15.7 1.0
CG B:ASP74 4.9 27.2 1.0
CA B:ASP118 5.0 13.8 1.0
C B:ASP118 5.0 14.3 1.0

Manganese binding site 4 out of 8 in 5oey

Go back to Manganese Binding Sites List in 5oey
Manganese binding site 4 out of 8 in the Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn703

b:21.0
occ:1.00
 O1 B:PO4701 1.5 45.3 1.0
OE2 B:GLU284 1.9 18.2 1.0
OE2 B:GLU97 2.1 22.6 1.0
OD2 B:ASP118 2.3 16.3 1.0
P B:PO4701 2.9 49.3 1.0
CD B:GLU97 3.0 20.1 1.0
CD B:GLU284 3.1 16.8 1.0
CG B:ASP118 3.1 14.2 1.0
OE1 B:GLU97 3.3 18.9 1.0
MN B:MN702 3.4 15.7 1.0
O2 B:PO4701 3.5 40.9 1.0
OD1 B:ASP118 3.5 13.8 1.0
OD1 B:ASP121 3.5 39.9 1.0
O3 B:PO4701 3.6 42.3 1.0
O4 B:PO4701 3.9 39.1 1.0
CG B:GLU284 3.9 16.0 1.0
OE1 B:GLU284 4.0 16.2 1.0
O B:HOH835 4.1 20.0 1.0
CB B:ASP118 4.3 14.1 1.0
CG B:GLU97 4.4 20.1 1.0
CG B:ASP121 4.5 35.4 1.0
CA B:ASP121 4.5 27.4 1.0
CB B:ASP121 4.5 30.4 1.0
O B:HOH823 4.6 17.2 1.0
O B:LEU120 4.9 21.5 1.0

Manganese binding site 5 out of 8 in 5oey

Go back to Manganese Binding Sites List in 5oey
Manganese binding site 5 out of 8 in the Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn702

b:31.4
occ:1.00
 O4 C:PO4701 1.6 41.5 1.0
O C:HOH801 1.8 33.9 1.0
OD1 C:ASP118 2.1 24.0 1.0
OE1 C:GLU97 2.1 34.1 1.0
O C:LEU120 2.3 25.9 1.0
CG C:ASP118 2.9 21.9 1.0
OD2 C:ASP118 3.0 20.6 1.0
P C:PO4701 3.1 38.4 1.0
C C:LEU120 3.2 24.6 1.0
CD C:GLU97 3.2 34.6 1.0
MN C:MN703 3.6 21.0 1.0
O1 C:PO4701 3.6 41.6 1.0
K C:K704 3.6 25.9 1.0
OE2 C:GLU97 3.7 34.7 1.0
OE2 C:GLU98 3.7 36.7 1.0
CA C:ASP121 3.8 29.1 1.0
N C:ASP121 3.8 26.6 1.0
O2 C:PO4701 3.9 35.2 1.0
OD1 C:ASP74 4.0 37.9 1.0
O3 C:PO4701 4.0 39.4 1.0
N C:LEU120 4.2 21.5 1.0
CA C:LEU120 4.2 23.2 1.0
OG C:SER123 4.3 48.9 1.0
CB C:ASP118 4.3 22.2 1.0
CG C:GLU97 4.5 34.1 1.0
CB C:ASP121 4.6 29.3 1.0
CB C:GLU97 4.8 34.1 1.0
CA C:ASP118 4.8 21.9 1.0
C C:ASP121 4.8 30.0 1.0
N C:GLY122 4.9 33.1 1.0
OE2 C:GLU284 4.9 24.4 1.0
NH1 C:ARG280 4.9 40.8 1.0
C C:ASP118 4.9 21.3 1.0
CB C:LEU120 4.9 23.8 1.0
CD C:GLU98 4.9 35.6 1.0
CD C:PRO119 5.0 23.1 1.0

Manganese binding site 6 out of 8 in 5oey

Go back to Manganese Binding Sites List in 5oey
Manganese binding site 6 out of 8 in the Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn703

b:21.0
occ:1.00
 OD2 C:ASP118 2.1 20.6 1.0
OE2 C:GLU284 2.2 24.4 1.0
OD1 C:ASP121 2.2 27.0 1.0
O2 C:PO4701 2.2 35.2 1.0
O4 C:PO4701 2.9 41.5 1.0
P C:PO4701 3.0 38.4 1.0
CG C:ASP121 3.1 30.3 1.0
CG C:ASP118 3.3 21.9 1.0
CD C:GLU284 3.3 23.9 1.0
CB C:ASP121 3.4 29.3 1.0
MN C:MN702 3.6 31.4 1.0
CA C:ASP121 3.6 29.1 1.0
O1 C:PO4701 3.6 41.6 1.0
OD1 C:ASP118 3.9 24.0 1.0
CG C:GLU284 3.9 23.6 1.0
OE1 C:GLU97 4.1 34.1 1.0
OE1 C:GLU284 4.3 23.5 1.0
NH1 C:ARG280 4.3 40.8 1.0
OD2 C:ASP121 4.3 35.0 1.0
O3 C:PO4701 4.4 39.4 1.0
CB C:ASP118 4.4 22.2 1.0
N C:GLY122 4.4 33.1 1.0
O C:HOH824 4.4 14.3 1.0
C C:ASP121 4.5 30.0 1.0
N C:ASP121 4.6 26.6 1.0
O C:LEU120 4.8 25.9 1.0
O C:HOH828 4.8 39.0 1.0
CD1 C:ILE135 4.9 14.5 1.0

Manganese binding site 7 out of 8 in 5oey

Go back to Manganese Binding Sites List in 5oey
Manganese binding site 7 out of 8 in the Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 7 of Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn702

b:70.9
occ:1.00
 OD2 D:ASP74 2.7 56.1 1.0
O3 D:PO4701 2.8 85.5 1.0
OE2 D:GLU98 2.8 56.7 1.0
OE1 D:GLU98 2.9 78.8 1.0
CD D:GLU98 3.2 64.4 1.0
O2 D:PO4701 3.5 84.7 1.0
K D:K704 3.5 12.9 1.0
O D:HOH803 3.7 13.6 1.0
CG D:ASP74 3.7 53.4 1.0
P D:PO4701 3.8 83.4 1.0
OE2 D:GLU97 4.0 37.6 1.0
OD1 D:ASP74 4.5 61.0 1.0
CB D:ASP74 4.5 48.6 1.0
OG D:SER123 4.7 39.0 1.0
O4 D:PO4701 4.7 81.5 1.0
CG D:GLU98 4.7 59.7 1.0
CD D:GLU97 4.9 36.9 1.0
O1 D:PO4701 4.9 87.5 1.0
CG D:GLU97 4.9 39.2 1.0

Manganese binding site 8 out of 8 in 5oey

Go back to Manganese Binding Sites List in 5oey
Manganese binding site 8 out of 8 in the Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 8 of Crystal Structure of Leishmania Major Fructose-1,6-Bisphosphatase in Holo Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn703

b:27.5
occ:1.00
 OE2 D:GLU284 1.9 27.8 1.0
O4 D:PO4701 1.9 81.5 1.0
OD2 D:ASP118 2.2 20.8 1.0
OD1 D:ASP121 2.5 34.3 1.0
OE1 D:GLU97 2.7 36.2 1.0
OE2 D:GLU97 2.7 37.6 1.0
CD D:GLU97 3.1 36.9 1.0
CG D:ASP118 3.1 19.9 1.0
CD D:GLU284 3.1 24.8 1.0
P D:PO4701 3.2 83.4 1.0
OD1 D:ASP118 3.5 19.3 1.0
O3 D:PO4701 3.7 85.5 1.0
CG D:ASP121 3.7 39.0 1.0
K D:K704 3.8 12.9 1.0
CG D:GLU284 3.9 23.7 1.0
O1 D:PO4701 3.9 87.5 1.0
OE1 D:GLU284 4.0 23.3 1.0
CB D:ASP118 4.2 19.6 1.0
CB D:ASP121 4.3 37.8 1.0
O2 D:PO4701 4.3 84.7 1.0
CA D:ASP121 4.3 35.6 1.0
CG D:GLU97 4.5 39.2 1.0
NH1 D:ARG280 4.6 41.9 1.0
OD2 D:ASP121 4.8 42.4 1.0
O D:LEU120 4.9 27.1 1.0

Reference:

M.Yuan, M.G.Vasquez-Valdivieso, I.W.Mcnae, P.A.M.Michels, L.A.Fothergill-Gilmore, M.D.Walkinshaw. Structures of Leishmania Fructose-1,6-Bisphosphatase Reveal Species-Specific Differences in the Mechanism of Allosteric Inhibition. J. Mol. Biol. V. 429 3075 2017.
ISSN: ESSN 1089-8638
PubMed: 28882541
DOI: 10.1016/J.JMB.2017.08.010
Page generated: Tue Dec 15 04:45:31 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