Magnesium in PDB 1p48: Reverse Protonation Is the Key to General Acid-Base Catalysis in Enolase
Enzymatic activity of Reverse Protonation Is the Key to General Acid-Base Catalysis in Enolase
All present enzymatic activity of Reverse Protonation Is the Key to General Acid-Base Catalysis in Enolase:
4.2.1.11;
Protein crystallography data
The structure of Reverse Protonation Is the Key to General Acid-Base Catalysis in Enolase, PDB code: 1p48
was solved by
P.A.Sims,
T.M.Larsen,
R.R.Poyner,
W.W.Cleland,
G.H.Reed,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
2.00
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
107.800,
114.500,
73.100,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
18.5 /
21.3
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Reverse Protonation Is the Key to General Acid-Base Catalysis in Enolase
(pdb code 1p48). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the
Reverse Protonation Is the Key to General Acid-Base Catalysis in Enolase, PDB code: 1p48:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 1p48
Go back to
Magnesium Binding Sites List in 1p48
Magnesium binding site 1 out
of 4 in the Reverse Protonation Is the Key to General Acid-Base Catalysis in Enolase
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Reverse Protonation Is the Key to General Acid-Base Catalysis in Enolase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg438
b:11.4
occ:1.00
|
OE2
|
A:GLU295
|
2.0
|
8.4
|
1.0
|
OD2
|
A:ASP320
|
2.0
|
8.4
|
1.0
|
O
|
A:HOH1003
|
2.1
|
1.9
|
1.0
|
O1
|
A:PEP440
|
2.2
|
6.8
|
1.0
|
OD2
|
A:ASP246
|
2.5
|
11.5
|
1.0
|
O2'
|
A:PEP440
|
2.6
|
8.6
|
1.0
|
C1
|
A:PEP440
|
2.7
|
8.5
|
1.0
|
CG
|
A:ASP320
|
3.0
|
10.3
|
1.0
|
CD
|
A:GLU295
|
3.2
|
7.2
|
1.0
|
CG
|
A:ASP246
|
3.3
|
10.8
|
1.0
|
OD1
|
A:ASP246
|
3.3
|
10.6
|
1.0
|
CB
|
A:ASP320
|
3.4
|
8.4
|
1.0
|
O
|
A:HOH1001
|
3.7
|
2.1
|
1.0
|
OD2
|
A:ASP296
|
3.9
|
8.8
|
1.0
|
CD2
|
A:LEU343
|
3.9
|
3.4
|
1.0
|
OE1
|
A:GLU295
|
3.9
|
7.0
|
1.0
|
O
|
A:HOH1002
|
3.9
|
16.1
|
1.0
|
NZ
|
A:LYS396
|
4.0
|
7.0
|
1.0
|
NZ
|
A:LYS345
|
4.0
|
3.8
|
1.0
|
CG
|
A:GLU295
|
4.1
|
7.4
|
1.0
|
OD1
|
A:ASP320
|
4.1
|
11.8
|
1.0
|
C2
|
A:PEP440
|
4.2
|
8.1
|
1.0
|
MG
|
A:MG439
|
4.3
|
17.9
|
1.0
|
CB
|
A:ASP246
|
4.7
|
7.9
|
1.0
|
NE2
|
A:GLN167
|
4.7
|
10.2
|
1.0
|
CG
|
A:ASP296
|
4.8
|
10.1
|
1.0
|
CE
|
A:LYS345
|
4.9
|
8.2
|
1.0
|
CA
|
A:ASP320
|
5.0
|
9.3
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 1p48
Go back to
Magnesium Binding Sites List in 1p48
Magnesium binding site 2 out
of 4 in the Reverse Protonation Is the Key to General Acid-Base Catalysis in Enolase
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Reverse Protonation Is the Key to General Acid-Base Catalysis in Enolase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg439
b:17.9
occ:1.00
|
O
|
A:SER39
|
2.1
|
20.5
|
1.0
|
O
|
A:HOH1001
|
2.1
|
2.1
|
1.0
|
OG
|
A:SER39
|
2.2
|
24.0
|
1.0
|
O1P
|
A:PEP440
|
2.3
|
7.8
|
1.0
|
O
|
A:HOH1002
|
2.3
|
16.1
|
1.0
|
O2'
|
A:PEP440
|
2.6
|
8.6
|
1.0
|
C
|
A:SER39
|
2.9
|
19.7
|
1.0
|
CB
|
A:SER39
|
2.9
|
21.2
|
1.0
|
P
|
A:PEP440
|
3.4
|
8.4
|
1.0
|
CA
|
A:SER39
|
3.4
|
19.9
|
1.0
|
C1
|
A:PEP440
|
3.5
|
8.5
|
1.0
|
O2
|
A:PEP440
|
3.6
|
8.2
|
1.0
|
O2P
|
A:PEP440
|
3.8
|
7.2
|
1.0
|
N
|
A:SER39
|
3.9
|
19.0
|
1.0
|
N
|
A:THR40
|
4.0
|
17.8
|
1.0
|
OD1
|
A:ASP321
|
4.0
|
8.9
|
1.0
|
C2
|
A:PEP440
|
4.1
|
8.1
|
1.0
|
NZ
|
A:LYS345
|
4.1
|
3.8
|
1.0
|
OD2
|
A:ASP320
|
4.1
|
8.4
|
1.0
|
OD2
|
A:ASP321
|
4.1
|
10.1
|
1.0
|
MG
|
A:MG438
|
4.3
|
11.4
|
1.0
|
NH2
|
A:ARG374
|
4.4
|
3.8
|
1.0
|
O
|
A:HOH1003
|
4.5
|
1.9
|
1.0
|
O1
|
A:PEP440
|
4.5
|
6.8
|
1.0
|
CG
|
A:ASP321
|
4.5
|
9.3
|
1.0
|
CA
|
A:THR40
|
4.5
|
16.0
|
1.0
|
NE2
|
A:GLN167
|
4.6
|
10.2
|
1.0
|
O3P
|
A:PEP440
|
4.6
|
6.7
|
1.0
|
OE1
|
A:GLN167
|
4.7
|
8.6
|
1.0
|
O
|
A:HOH1547
|
5.0
|
23.3
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 1p48
Go back to
Magnesium Binding Sites List in 1p48
Magnesium binding site 3 out
of 4 in the Reverse Protonation Is the Key to General Acid-Base Catalysis in Enolase
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Reverse Protonation Is the Key to General Acid-Base Catalysis in Enolase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg938
b:7.6
occ:1.00
|
OE2
|
B:GLU795
|
2.1
|
10.6
|
1.0
|
OD2
|
B:ASP820
|
2.1
|
5.1
|
1.0
|
O
|
B:HOH1006
|
2.2
|
9.3
|
1.0
|
O1
|
B:PEP940
|
2.2
|
7.1
|
1.0
|
OD2
|
B:ASP746
|
2.2
|
8.6
|
1.0
|
O2'
|
B:PEP940
|
2.4
|
10.6
|
1.0
|
C1
|
B:PEP940
|
2.6
|
8.0
|
1.0
|
CG
|
B:ASP746
|
3.0
|
11.6
|
1.0
|
CG
|
B:ASP820
|
3.2
|
7.6
|
1.0
|
OD1
|
B:ASP746
|
3.2
|
10.1
|
1.0
|
CD
|
B:GLU795
|
3.2
|
9.9
|
1.0
|
CB
|
B:ASP820
|
3.6
|
5.9
|
1.0
|
O
|
B:HOH1004
|
3.7
|
2.8
|
1.0
|
NZ
|
B:LYS896
|
3.8
|
6.8
|
1.0
|
OE1
|
B:GLU795
|
4.0
|
7.8
|
1.0
|
O
|
B:HOH1005
|
4.0
|
12.8
|
1.0
|
OD2
|
B:ASP796
|
4.1
|
10.8
|
1.0
|
CD2
|
B:LEU843
|
4.1
|
6.5
|
1.0
|
C2
|
B:PEP940
|
4.1
|
7.9
|
1.0
|
NZ
|
B:LYS845
|
4.1
|
6.0
|
1.0
|
MG
|
B:MG939
|
4.2
|
21.1
|
1.0
|
CG
|
B:GLU795
|
4.2
|
7.2
|
1.0
|
OD1
|
B:ASP820
|
4.2
|
6.8
|
1.0
|
CB
|
B:ASP746
|
4.4
|
6.7
|
1.0
|
NE2
|
B:GLN667
|
4.7
|
8.5
|
1.0
|
CG
|
B:ASP796
|
4.9
|
9.7
|
1.0
|
OE2
|
B:GLU668
|
4.9
|
6.8
|
1.0
|
O2
|
B:PEP940
|
5.0
|
8.4
|
1.0
|
CE
|
B:LYS896
|
5.0
|
6.0
|
1.0
|
C3
|
B:PEP940
|
5.0
|
8.4
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 1p48
Go back to
Magnesium Binding Sites List in 1p48
Magnesium binding site 4 out
of 4 in the Reverse Protonation Is the Key to General Acid-Base Catalysis in Enolase
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Reverse Protonation Is the Key to General Acid-Base Catalysis in Enolase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg939
b:21.1
occ:1.00
|
O
|
B:HOH1004
|
2.1
|
2.8
|
1.0
|
O
|
B:SER539
|
2.1
|
14.8
|
1.0
|
OG
|
B:SER539
|
2.2
|
12.3
|
1.0
|
O
|
B:HOH1005
|
2.2
|
12.8
|
1.0
|
O1P
|
B:PEP940
|
2.3
|
8.7
|
1.0
|
O2'
|
B:PEP940
|
2.3
|
10.6
|
1.0
|
CB
|
B:SER539
|
3.0
|
13.9
|
1.0
|
C
|
B:SER539
|
3.0
|
13.3
|
1.0
|
C1
|
B:PEP940
|
3.3
|
8.0
|
1.0
|
P
|
B:PEP940
|
3.4
|
9.0
|
1.0
|
CA
|
B:SER539
|
3.5
|
13.5
|
1.0
|
O2
|
B:PEP940
|
3.5
|
8.4
|
1.0
|
O2P
|
B:PEP940
|
3.9
|
11.7
|
1.0
|
C2
|
B:PEP940
|
4.0
|
7.9
|
1.0
|
N
|
B:SER539
|
4.0
|
13.2
|
1.0
|
OD2
|
B:ASP820
|
4.0
|
5.1
|
1.0
|
N
|
B:THR540
|
4.1
|
13.1
|
1.0
|
OD2
|
B:ASP821
|
4.1
|
10.8
|
1.0
|
OD1
|
B:ASP821
|
4.2
|
8.8
|
1.0
|
NZ
|
B:LYS845
|
4.2
|
6.0
|
1.0
|
MG
|
B:MG938
|
4.2
|
7.6
|
1.0
|
O
|
B:HOH1006
|
4.3
|
9.3
|
1.0
|
O1
|
B:PEP940
|
4.4
|
7.1
|
1.0
|
OE1
|
B:GLN667
|
4.4
|
10.0
|
1.0
|
NE2
|
B:GLN667
|
4.5
|
8.5
|
1.0
|
NH2
|
B:ARG874
|
4.5
|
6.8
|
1.0
|
CG
|
B:ASP821
|
4.6
|
10.0
|
1.0
|
O3P
|
B:PEP940
|
4.7
|
6.9
|
1.0
|
CA
|
B:THR540
|
4.7
|
12.4
|
1.0
|
CD
|
B:GLN667
|
4.9
|
9.2
|
1.0
|
|
Reference:
P.A.Sims,
T.M.Larsen,
R.R.Poyner,
W.W.Cleland,
G.H.Reed.
Reverse Protonation Is the Key to General Acid-Base Catalysis in Enolase Biochemistry V. 42 8298 2003.
ISSN: ISSN 0006-2960
PubMed: 12846578
DOI: 10.1021/BI0346345
Page generated: Tue Aug 13 10:47:55 2024
|