Magnesium in PDB 1p43: 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: 1p43
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 /
1.80
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
107.300,
115.100,
72.400,
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 1p43). 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: 1p43:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 1p43
Go back to
Magnesium Binding Sites List in 1p43
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:13.1
occ:1.00
|
OE2
|
A:GLU295
|
2.0
|
9.7
|
1.0
|
O
|
A:HOH1002
|
2.1
|
10.9
|
1.0
|
OD2
|
A:ASP320
|
2.1
|
10.5
|
1.0
|
O1
|
A:2PG441
|
2.3
|
16.5
|
1.0
|
OD2
|
A:ASP246
|
2.4
|
14.3
|
1.0
|
O2
|
A:2PG441
|
2.5
|
18.9
|
1.0
|
C1
|
A:2PG441
|
2.7
|
16.9
|
1.0
|
CG
|
A:ASP320
|
3.1
|
11.0
|
1.0
|
CG
|
A:ASP246
|
3.2
|
13.7
|
1.0
|
CD
|
A:GLU295
|
3.2
|
8.4
|
1.0
|
OD1
|
A:ASP246
|
3.3
|
13.6
|
1.0
|
CB
|
A:ASP320
|
3.6
|
10.3
|
1.0
|
NZ
|
A:LYS396
|
3.8
|
12.9
|
1.0
|
O
|
A:HOH1001
|
3.8
|
6.5
|
1.0
|
OE1
|
A:GLU295
|
3.9
|
8.9
|
1.0
|
OD2
|
A:ASP296
|
4.1
|
14.2
|
1.0
|
CD2
|
A:LEU343
|
4.1
|
8.3
|
1.0
|
CG
|
A:GLU295
|
4.1
|
9.6
|
1.0
|
NZ
|
A:LYS345
|
4.2
|
11.6
|
1.0
|
OD1
|
A:ASP320
|
4.2
|
12.1
|
1.0
|
C2
|
A:2PG441
|
4.3
|
17.2
|
1.0
|
CB
|
A:ASP246
|
4.6
|
11.3
|
1.0
|
CG
|
A:ASP296
|
4.9
|
12.8
|
1.0
|
O1P
|
A:2PG441
|
4.9
|
15.2
|
1.0
|
O
|
A:HOH1004
|
4.9
|
32.9
|
1.0
|
CE
|
A:LYS345
|
5.0
|
12.6
|
1.0
|
OE1
|
A:GLN168
|
5.0
|
17.9
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 1p43
Go back to
Magnesium Binding Sites List in 1p43
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:28.0
occ:1.00
|
O
|
A:HOH1867
|
2.2
|
33.1
|
1.0
|
O
|
A:SER39
|
2.4
|
26.9
|
1.0
|
O
|
A:HOH1001
|
2.5
|
6.5
|
1.0
|
O3P
|
A:2PG441
|
2.6
|
12.1
|
1.0
|
O
|
A:HOH1003
|
3.1
|
26.7
|
1.0
|
O
|
A:HOH1004
|
3.3
|
32.9
|
1.0
|
C
|
A:SER39
|
3.4
|
26.0
|
1.0
|
OD1
|
A:ASP321
|
3.5
|
17.6
|
1.0
|
P
|
A:2PG441
|
3.8
|
10.4
|
1.0
|
O4P
|
A:2PG441
|
3.9
|
13.4
|
1.0
|
O1
|
A:2PG441
|
3.9
|
16.5
|
1.0
|
OD2
|
A:ASP321
|
3.9
|
18.6
|
1.0
|
NZ
|
A:LYS345
|
4.1
|
11.6
|
1.0
|
CG
|
A:ASP321
|
4.1
|
16.2
|
1.0
|
N
|
A:THR40
|
4.2
|
24.4
|
1.0
|
CA
|
A:SER39
|
4.2
|
25.9
|
1.0
|
CB
|
A:SER39
|
4.3
|
27.2
|
1.0
|
CA
|
A:THR40
|
4.3
|
24.1
|
1.0
|
N
|
A:SER39
|
4.4
|
24.4
|
1.0
|
O1P
|
A:2PG441
|
4.4
|
15.2
|
1.0
|
OD2
|
A:ASP320
|
4.4
|
10.5
|
1.0
|
NH2
|
A:ARG374
|
4.5
|
12.0
|
1.0
|
C1
|
A:2PG441
|
4.7
|
16.9
|
1.0
|
OG
|
A:SER39
|
4.7
|
30.2
|
1.0
|
N
|
A:GLY41
|
4.8
|
23.2
|
1.0
|
C
|
A:THR40
|
4.8
|
23.6
|
1.0
|
OE2
|
A:GLU44
|
4.8
|
19.0
|
1.0
|
O
|
A:HOH1002
|
5.0
|
10.9
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 1p43
Go back to
Magnesium Binding Sites List in 1p43
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:7.5
occ:1.00
|
OE2
|
B:GLU795
|
2.0
|
9.0
|
1.0
|
OD2
|
B:ASP820
|
2.1
|
8.7
|
1.0
|
O
|
B:HOH1007
|
2.2
|
8.8
|
1.0
|
OD2
|
B:ASP746
|
2.2
|
9.9
|
1.0
|
O1
|
B:2PG941
|
2.3
|
14.0
|
1.0
|
O2
|
B:2PG941
|
2.3
|
17.6
|
1.0
|
C1
|
B:2PG941
|
2.6
|
12.8
|
1.0
|
CG
|
B:ASP746
|
3.0
|
11.1
|
1.0
|
CD
|
B:GLU795
|
3.1
|
7.9
|
1.0
|
CG
|
B:ASP820
|
3.2
|
8.4
|
1.0
|
OD1
|
B:ASP746
|
3.3
|
9.9
|
1.0
|
CB
|
B:ASP820
|
3.7
|
7.8
|
1.0
|
O
|
B:HOH1005
|
3.7
|
1.0
|
1.0
|
OE1
|
B:GLU795
|
3.9
|
8.6
|
1.0
|
NZ
|
B:LYS896
|
3.9
|
8.5
|
1.0
|
OD2
|
B:ASP796
|
4.0
|
9.8
|
1.0
|
CD2
|
B:LEU843
|
4.1
|
8.3
|
1.0
|
NZ
|
B:LYS845
|
4.1
|
9.5
|
1.0
|
CG
|
B:GLU795
|
4.1
|
7.2
|
1.0
|
C2
|
B:2PG941
|
4.2
|
15.3
|
1.0
|
OD1
|
B:ASP820
|
4.3
|
8.7
|
1.0
|
CB
|
B:ASP746
|
4.4
|
10.1
|
1.0
|
CG
|
B:ASP796
|
4.8
|
6.8
|
1.0
|
O1P
|
B:2PG941
|
4.9
|
12.6
|
1.0
|
O3
|
B:2PG941
|
5.0
|
25.1
|
1.0
|
O
|
B:HOH1516
|
5.0
|
35.5
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 1p43
Go back to
Magnesium Binding Sites List in 1p43
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:27.1
occ:1.00
|
O
|
B:HOH1006
|
2.3
|
32.1
|
1.0
|
O
|
B:HOH1005
|
2.4
|
1.0
|
1.0
|
O
|
B:SER539
|
2.5
|
23.4
|
1.0
|
O3P
|
B:2PG941
|
2.6
|
9.9
|
1.0
|
O
|
B:HOH1516
|
3.1
|
35.5
|
1.0
|
O
|
B:HOH1515
|
3.2
|
27.2
|
1.0
|
C
|
B:SER539
|
3.3
|
21.4
|
1.0
|
P
|
B:2PG941
|
3.7
|
8.5
|
1.0
|
OD1
|
B:ASP821
|
3.7
|
13.5
|
1.0
|
O1
|
B:2PG941
|
3.8
|
14.0
|
1.0
|
O4P
|
B:2PG941
|
3.8
|
8.8
|
1.0
|
N
|
B:THR540
|
4.0
|
18.7
|
1.0
|
CA
|
B:THR540
|
4.1
|
15.8
|
1.0
|
OD2
|
B:ASP821
|
4.2
|
14.2
|
1.0
|
CA
|
B:SER539
|
4.2
|
22.1
|
1.0
|
N
|
B:SER539
|
4.3
|
21.4
|
1.0
|
O1P
|
B:2PG941
|
4.3
|
12.6
|
1.0
|
CB
|
B:SER539
|
4.3
|
23.1
|
1.0
|
O
|
B:HOH1782
|
4.3
|
34.1
|
1.0
|
NH2
|
B:ARG874
|
4.3
|
9.4
|
1.0
|
CG
|
B:ASP821
|
4.4
|
13.5
|
1.0
|
NZ
|
B:LYS845
|
4.4
|
9.5
|
1.0
|
C
|
B:THR540
|
4.6
|
16.1
|
1.0
|
C1
|
B:2PG941
|
4.6
|
12.8
|
1.0
|
N
|
B:GLY541
|
4.6
|
14.9
|
1.0
|
OD2
|
B:ASP820
|
4.7
|
8.7
|
1.0
|
O
|
B:HOH1797
|
4.7
|
44.9
|
1.0
|
OE2
|
B:GLU544
|
4.9
|
9.8
|
1.0
|
C2
|
B:2PG941
|
4.9
|
15.3
|
1.0
|
OG
|
B:SER539
|
5.0
|
26.0
|
1.0
|
O2P
|
B:2PG941
|
5.0
|
7.1
|
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 10:47:43 2024
|