Manganese in PDB 3nvt: 1.95 Angstrom Crystal Structure of A Bifunctional 3-Deoxy-7- Phosphoheptulonate Synthase/Chorismate Mutase (Aroa) From Listeria Monocytogenes Egd-E
Enzymatic activity of 1.95 Angstrom Crystal Structure of A Bifunctional 3-Deoxy-7- Phosphoheptulonate Synthase/Chorismate Mutase (Aroa) From Listeria Monocytogenes Egd-E
All present enzymatic activity of 1.95 Angstrom Crystal Structure of A Bifunctional 3-Deoxy-7- Phosphoheptulonate Synthase/Chorismate Mutase (Aroa) From Listeria Monocytogenes Egd-E:
2.5.1.54;
5.4.99.5;
Protein crystallography data
The structure of 1.95 Angstrom Crystal Structure of A Bifunctional 3-Deoxy-7- Phosphoheptulonate Synthase/Chorismate Mutase (Aroa) From Listeria Monocytogenes Egd-E, PDB code: 3nvt
was solved by
A.S.Halavaty,
S.H.Light,
G.Minasov,
L.Shuvalova,
K.Kwon,
W.F.Anderson,
Center For Structural Genomics Of Infectious Diseases (Csgid),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.04 /
1.95
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
111.570,
111.787,
81.049,
90.00,
127.63,
90.00
|
R / Rfree (%)
|
15.4 /
19.8
|
Manganese Binding Sites:
The binding sites of Manganese atom in the 1.95 Angstrom Crystal Structure of A Bifunctional 3-Deoxy-7- Phosphoheptulonate Synthase/Chorismate Mutase (Aroa) From Listeria Monocytogenes Egd-E
(pdb code 3nvt). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the
1.95 Angstrom Crystal Structure of A Bifunctional 3-Deoxy-7- Phosphoheptulonate Synthase/Chorismate Mutase (Aroa) From Listeria Monocytogenes Egd-E, PDB code: 3nvt:
Jump to Manganese binding site number:
1;
2;
3;
4;
Manganese binding site 1 out
of 4 in 3nvt
Go back to
Manganese Binding Sites List in 3nvt
Manganese binding site 1 out
of 4 in the 1.95 Angstrom Crystal Structure of A Bifunctional 3-Deoxy-7- Phosphoheptulonate Synthase/Chorismate Mutase (Aroa) From Listeria Monocytogenes Egd-E
 Mono view
 Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of 1.95 Angstrom Crystal Structure of A Bifunctional 3-Deoxy-7- Phosphoheptulonate Synthase/Chorismate Mutase (Aroa) From Listeria Monocytogenes Egd-E within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn362
b:18.7
occ:0.60
|
MN
|
A:MN362
|
0.0
|
18.7
|
0.6
|
MN
|
A:MN362
|
1.4
|
29.1
|
0.4
|
OD2
|
A:ASP333
|
2.0
|
44.4
|
1.0
|
OE1
|
A:GLU322
|
2.1
|
33.7
|
1.0
|
NE2
|
A:HIS296
|
2.1
|
29.3
|
1.0
|
SG
|
A:CYS126
|
2.5
|
30.8
|
1.0
|
OE2
|
A:GLU322
|
2.5
|
38.4
|
1.0
|
CD
|
A:GLU322
|
2.6
|
33.0
|
1.0
|
CE1
|
A:HIS296
|
2.9
|
32.1
|
1.0
|
CG
|
A:ASP333
|
3.0
|
44.6
|
1.0
|
CD2
|
A:HIS296
|
3.1
|
28.4
|
1.0
|
CB
|
A:CYS126
|
3.1
|
27.8
|
1.0
|
O
|
A:HOH695
|
3.3
|
67.4
|
1.0
|
CB
|
A:ASP333
|
3.6
|
38.3
|
1.0
|
CA
|
A:CYS126
|
4.0
|
26.8
|
1.0
|
ND1
|
A:HIS296
|
4.0
|
31.0
|
1.0
|
CG
|
A:GLU322
|
4.1
|
28.9
|
1.0
|
OD1
|
A:ASP333
|
4.1
|
46.9
|
1.0
|
CG
|
A:HIS296
|
4.2
|
25.6
|
1.0
|
CH3
|
A:ACT363
|
4.4
|
46.6
|
1.0
|
CG2
|
A:THR295
|
4.5
|
21.3
|
1.0
|
NH2
|
A:ARG150
|
4.6
|
44.0
|
0.6
|
CB
|
A:GLU322
|
4.8
|
22.8
|
1.0
|
N
|
A:CYS126
|
4.9
|
25.9
|
1.0
|
|
Manganese binding site 2 out
of 4 in 3nvt
Go back to
Manganese Binding Sites List in 3nvt
Manganese binding site 2 out
of 4 in the 1.95 Angstrom Crystal Structure of A Bifunctional 3-Deoxy-7- Phosphoheptulonate Synthase/Chorismate Mutase (Aroa) From Listeria Monocytogenes Egd-E
 Mono view
 Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of 1.95 Angstrom Crystal Structure of A Bifunctional 3-Deoxy-7- Phosphoheptulonate Synthase/Chorismate Mutase (Aroa) From Listeria Monocytogenes Egd-E within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn362
b:29.1
occ:0.40
|
MN
|
A:MN362
|
0.0
|
29.1
|
0.4
|
MN
|
A:MN362
|
1.4
|
18.7
|
0.6
|
NE2
|
A:HIS296
|
2.0
|
29.3
|
1.0
|
SG
|
A:CYS126
|
2.2
|
30.8
|
1.0
|
OE2
|
A:GLU322
|
2.3
|
38.4
|
1.0
|
CE1
|
A:HIS296
|
2.5
|
32.1
|
1.0
|
CD
|
A:GLU322
|
3.0
|
33.0
|
1.0
|
OE1
|
A:GLU322
|
3.0
|
33.7
|
1.0
|
O
|
A:HOH695
|
3.1
|
67.4
|
1.0
|
OD2
|
A:ASP333
|
3.2
|
44.4
|
1.0
|
CH3
|
A:ACT363
|
3.2
|
46.6
|
1.0
|
CB
|
A:CYS126
|
3.3
|
27.8
|
1.0
|
CD2
|
A:HIS296
|
3.3
|
28.4
|
1.0
|
NH2
|
A:ARG150
|
3.7
|
44.0
|
0.6
|
CA
|
A:CYS126
|
3.7
|
26.8
|
1.0
|
ND1
|
A:HIS296
|
3.8
|
31.0
|
1.0
|
C
|
A:ACT363
|
3.8
|
46.4
|
1.0
|
NZ
|
A:LYS155
|
3.9
|
33.6
|
1.0
|
CG
|
A:HIS296
|
4.2
|
25.6
|
1.0
|
NH2
|
A:ARG150
|
4.2
|
24.7
|
0.4
|
CG
|
A:ASP333
|
4.2
|
44.6
|
1.0
|
OXT
|
A:ACT363
|
4.2
|
47.2
|
1.0
|
CG
|
A:GLU322
|
4.4
|
28.9
|
1.0
|
O
|
A:CYS126
|
4.4
|
26.6
|
1.0
|
C
|
A:CYS126
|
4.5
|
27.6
|
1.0
|
O
|
A:ACT363
|
4.5
|
46.4
|
1.0
|
CZ
|
A:ARG150
|
4.6
|
26.3
|
0.4
|
O
|
A:HOH697
|
4.7
|
99.3
|
1.0
|
CB
|
A:ASP333
|
4.8
|
38.3
|
1.0
|
NH1
|
A:ARG150
|
4.8
|
25.3
|
0.4
|
CZ
|
A:ARG150
|
4.8
|
42.8
|
0.6
|
N
|
A:CYS126
|
4.9
|
25.9
|
1.0
|
CE
|
A:LYS155
|
4.9
|
34.9
|
1.0
|
|
Manganese binding site 3 out
of 4 in 3nvt
Go back to
Manganese Binding Sites List in 3nvt
Manganese binding site 3 out
of 4 in the 1.95 Angstrom Crystal Structure of A Bifunctional 3-Deoxy-7- Phosphoheptulonate Synthase/Chorismate Mutase (Aroa) From Listeria Monocytogenes Egd-E
 Mono view
 Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of 1.95 Angstrom Crystal Structure of A Bifunctional 3-Deoxy-7- Phosphoheptulonate Synthase/Chorismate Mutase (Aroa) From Listeria Monocytogenes Egd-E within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn362
b:18.5
occ:0.70
|
MN
|
B:MN362
|
0.0
|
18.5
|
0.7
|
MN
|
B:MN362
|
1.3
|
22.4
|
0.3
|
OE1
|
B:GLU322
|
2.0
|
25.5
|
1.0
|
OD2
|
B:ASP333
|
2.1
|
34.2
|
1.0
|
NE2
|
B:HIS296
|
2.1
|
27.8
|
1.0
|
SG
|
B:CYS126
|
2.4
|
23.0
|
1.0
|
OE2
|
B:GLU322
|
2.5
|
28.4
|
1.0
|
CD
|
B:GLU322
|
2.6
|
26.0
|
1.0
|
CE1
|
B:HIS296
|
2.9
|
29.7
|
1.0
|
CB
|
B:CYS126
|
3.1
|
20.2
|
1.0
|
CG
|
B:ASP333
|
3.1
|
33.8
|
1.0
|
CD2
|
B:HIS296
|
3.2
|
26.2
|
1.0
|
CB
|
B:ASP333
|
3.6
|
27.4
|
1.0
|
CA
|
B:CYS126
|
4.0
|
20.3
|
1.0
|
ND1
|
B:HIS296
|
4.0
|
28.7
|
1.0
|
CG
|
B:GLU322
|
4.1
|
22.4
|
1.0
|
OD1
|
B:ASP333
|
4.1
|
36.5
|
1.0
|
CG
|
B:HIS296
|
4.2
|
23.8
|
1.0
|
NH2
|
B:ARG150
|
4.5
|
36.1
|
0.5
|
CG2
|
B:THR295
|
4.7
|
18.1
|
1.0
|
CB
|
B:GLU322
|
4.9
|
18.6
|
1.0
|
N
|
B:CYS126
|
4.9
|
19.5
|
1.0
|
|
Manganese binding site 4 out
of 4 in 3nvt
Go back to
Manganese Binding Sites List in 3nvt
Manganese binding site 4 out
of 4 in the 1.95 Angstrom Crystal Structure of A Bifunctional 3-Deoxy-7- Phosphoheptulonate Synthase/Chorismate Mutase (Aroa) From Listeria Monocytogenes Egd-E
 Mono view
 Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of 1.95 Angstrom Crystal Structure of A Bifunctional 3-Deoxy-7- Phosphoheptulonate Synthase/Chorismate Mutase (Aroa) From Listeria Monocytogenes Egd-E within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn362
b:22.4
occ:0.30
|
MN
|
B:MN362
|
0.0
|
22.4
|
0.3
|
MN
|
B:MN362
|
1.3
|
18.5
|
0.7
|
NE2
|
B:HIS296
|
2.1
|
27.8
|
1.0
|
OE2
|
B:GLU322
|
2.1
|
28.4
|
1.0
|
SG
|
B:CYS126
|
2.2
|
23.0
|
1.0
|
CE1
|
B:HIS296
|
2.5
|
29.7
|
1.0
|
CD
|
B:GLU322
|
2.8
|
26.0
|
1.0
|
OE1
|
B:GLU322
|
2.8
|
25.5
|
1.0
|
CB
|
B:CYS126
|
3.1
|
20.2
|
1.0
|
OD2
|
B:ASP333
|
3.3
|
34.2
|
1.0
|
CD2
|
B:HIS296
|
3.4
|
26.2
|
1.0
|
NH2
|
B:ARG150
|
3.6
|
36.1
|
0.5
|
CA
|
B:CYS126
|
3.6
|
20.3
|
1.0
|
ND1
|
B:HIS296
|
3.8
|
28.7
|
1.0
|
NZ
|
B:LYS155
|
4.0
|
25.7
|
1.0
|
NH2
|
B:ARG150
|
4.1
|
22.0
|
0.5
|
O
|
B:HOH526
|
4.2
|
28.2
|
1.0
|
CG
|
B:GLU322
|
4.2
|
22.4
|
1.0
|
CG
|
B:HIS296
|
4.2
|
23.8
|
1.0
|
CG
|
B:ASP333
|
4.3
|
33.8
|
1.0
|
C
|
B:CYS126
|
4.4
|
21.0
|
1.0
|
O
|
B:CYS126
|
4.5
|
20.5
|
1.0
|
CZ
|
B:ARG150
|
4.5
|
23.9
|
0.5
|
CZ
|
B:ARG150
|
4.7
|
33.9
|
0.5
|
N
|
B:CYS126
|
4.7
|
19.5
|
1.0
|
CB
|
B:ASP333
|
4.8
|
27.4
|
1.0
|
NH1
|
B:ARG150
|
4.8
|
24.1
|
0.5
|
CE
|
B:LYS155
|
5.0
|
26.9
|
1.0
|
|
Reference:
S.H.Light,
A.S.Halavaty,
G.Minasov,
L.Shuvalova,
W.F.Anderson.
Structural Analysis of A 3-Deoxy-D-Arabino-Heptulosonate 7-Phosphate Synthase with An N-Terminal Chorismate Mutase-Like Regulatory Domain. Protein Sci. V. 21 887 2012.
ISSN: ISSN 0961-8368
PubMed: 22505283
DOI: 10.1002/PRO.2075
Page generated: Sat Oct 5 17:21:27 2024
|