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Magnesium in PDB 2al2: Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0

Enzymatic activity of Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0

All present enzymatic activity of Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0:
4.2.1.11;

Protein crystallography data

The structure of Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0, PDB code: 2al2 was solved by P.A.Sims, A.L.Menefee, T.M.Larsen, S.O.Mansoorabadi, G.H.Reed, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.00 / 1.85
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 71.700, 65.600, 85.900, 90.00, 99.20, 90.00
R / Rfree (%) 19.6 / 26.7

Other elements in 2al2:

The structure of Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0 also contains other interesting chemical elements:

Potassium (K) 1 atom
Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0 (pdb code 2al2). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0, PDB code: 2al2:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 2al2

Go back to Magnesium Binding Sites List in 2al2
Magnesium binding site 1 out of 4 in the Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg438

b:10.8
occ:1.00
 O A:HOH1003 1.9 10.5 1.0
OE2 A:GLU295 2.0 12.1 1.0
OD2 A:ASP246 2.1 12.9 1.0
O2 A:2PG441 2.1 13.9 0.7
OD2 A:ASP320 2.1 14.0 1.0
O1 A:PEP440 2.2 12.0 0.3
O1 A:2PG441 2.4 12.7 0.7
O2' A:PEP440 2.6 12.2 0.3
C1 A:2PG441 2.6 12.8 0.7
C1 A:PEP440 2.7 12.7 0.3
CG A:ASP246 3.0 15.5 1.0
CD A:GLU295 3.0 12.4 1.0
CG A:ASP320 3.2 14.0 1.0
OD1 A:ASP246 3.3 9.3 1.0
CB A:ASP320 3.5 10.1 1.0
NZ A:LYS396 3.7 5.6 1.0
O A:HOH1002 3.8 10.6 1.0
OE1 A:GLU295 3.8 14.1 1.0
CG A:GLU295 3.9 7.3 1.0
CD2 A:LEU343 3.9 16.6 1.0
O A:HOH1001 4.0 14.5 1.0
C2 A:2PG441 4.1 8.9 0.7
OD2 A:ASP296 4.2 14.1 1.0
C2 A:PEP440 4.2 9.4 0.3
MG A:MG439 4.2 15.1 1.0
OD1 A:ASP320 4.3 11.8 1.0
CB A:ASP246 4.3 9.4 1.0
OE1 A:GLN167 4.3 19.1 1.0
OE2 A:GLU168 4.6 17.8 1.0
C3 A:2PG441 4.8 5.1 0.7
C3 A:PEP440 4.9 4.7 0.3
CG A:ASP296 4.9 12.4 1.0
O1P A:2PG441 5.0 11.2 0.7
CE A:LYS396 5.0 8.9 1.0

Magnesium binding site 2 out of 4 in 2al2

Go back to Magnesium Binding Sites List in 2al2
Magnesium binding site 2 out of 4 in the Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg439

b:15.1
occ:1.00
 O4P A:2PG441 1.9 10.2 0.7
O1P A:PEP440 2.0 10.2 0.3
OG A:SER39 2.0 12.6 1.0
O A:SER39 2.1 10.4 1.0
O A:HOH1002 2.1 10.6 1.0
O2' A:PEP440 2.1 12.2 0.3
O A:HOH1001 2.1 14.5 1.0
O1 A:2PG441 2.3 12.7 0.7
C A:SER39 3.0 10.5 1.0
CB A:SER39 3.0 12.3 1.0
C1 A:PEP440 3.0 12.7 0.3
P A:PEP440 3.1 10.9 0.3
P A:2PG441 3.2 9.9 0.7
C1 A:2PG441 3.3 12.8 0.7
CA A:SER39 3.4 9.1 1.0
O2 A:PEP440 3.5 10.5 0.3
O1P A:2PG441 3.5 11.2 0.7
C2 A:PEP440 3.7 9.4 0.3
C2 A:2PG441 3.7 8.9 0.7
O2P A:PEP440 3.7 9.1 0.3
OD2 A:ASP320 3.9 14.0 1.0
O2P A:2PG441 4.0 7.8 0.7
N A:SER39 4.0 13.2 1.0
O1 A:PEP440 4.0 12.0 0.3
N A:THR40 4.1 16.8 1.0
OD1 A:ASP321 4.1 19.8 1.0
OD2 A:ASP321 4.2 18.9 1.0
O A:HOH1003 4.2 10.5 1.0
MG A:MG438 4.2 10.8 1.0
NH2 A:ARG374 4.3 10.7 1.0
O2 A:2PG441 4.3 13.9 0.7
NE2 A:GLN167 4.3 6.6 1.0
OE1 A:GLN167 4.3 19.1 1.0
O3P A:2PG441 4.4 8.8 0.7
O3P A:PEP440 4.5 8.3 0.3
CG A:ASP321 4.6 19.4 1.0
CA A:THR40 4.6 11.1 1.0
CD A:GLN167 4.8 18.5 1.0
C3 A:PEP440 4.9 4.7 0.3
CG A:ASP320 5.0 14.0 1.0

Magnesium binding site 3 out of 4 in 2al2

Go back to Magnesium Binding Sites List in 2al2
Magnesium binding site 3 out of 4 in the Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg438

b:12.7
occ:1.00
 OE2 B:GLU295 1.8 16.7 1.0
O1 B:PEP440 2.0 15.1 0.5
O2 B:2PG441 2.0 13.0 0.5
OD2 B:ASP320 2.2 15.1 1.0
OD2 B:ASP246 2.2 17.6 1.0
O1 B:2PG441 2.2 10.4 0.5
O B:HOH1010 2.3 17.0 1.0
O2' B:PEP440 2.4 10.0 0.5
C1 B:2PG441 2.4 15.2 0.5
C1 B:PEP440 2.5 15.4 0.5
CD B:GLU295 3.0 12.0 1.0
CG B:ASP246 3.1 22.5 1.0
CG B:ASP320 3.3 19.3 1.0
OD1 B:ASP246 3.4 15.2 1.0
NZ B:LYS396 3.6 6.8 1.0
OE1 B:GLU295 3.7 18.6 1.0
CB B:ASP320 3.7 10.6 1.0
O B:HOH1112 3.8 13.2 1.0
CD2 B:LEU343 3.9 15.7 1.0
C2 B:2PG441 3.9 18.1 0.5
CG B:GLU295 4.0 10.4 1.0
C2 B:PEP440 4.0 16.4 0.5
NZ B:LYS345 4.0 19.6 1.0
OD2 B:ASP296 4.2 26.0 1.0
OE2 B:GLU168 4.2 43.7 1.0
O B:HOH1419 4.2 23.3 1.0
OD1 B:ASP320 4.3 20.0 1.0
CB B:ASP246 4.4 20.3 1.0
C3 B:2PG441 4.7 18.9 0.5
C3 B:PEP440 4.7 20.0 0.5
CE B:LYS396 4.8 14.6 1.0
O1P B:2PG441 4.8 15.3 0.5
O3 B:2PG441 4.9 24.0 0.5
O2 B:PEP440 4.9 15.0 0.5
CE B:LYS345 5.0 19.8 1.0

Magnesium binding site 4 out of 4 in 2al2

Go back to Magnesium Binding Sites List in 2al2
Magnesium binding site 4 out of 4 in the Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure Analysis of Enolase Mg Subunit Complex at pH 8.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg439

b:39.6
occ:1.00
 O4P B:2PG441 2.3 14.1 0.5
O B:HOH1521 2.4 35.4 1.0
O B:HOH1112 2.5 13.2 1.0
O1P B:PEP440 2.6 14.9 0.5
O B:HOH1419 2.6 23.3 1.0
O2' B:PEP440 3.5 10.0 0.5
N B:THR40 3.5 22.4 1.0
P B:2PG441 3.5 14.1 0.5
P B:PEP440 3.6 14.5 0.5
O1 B:2PG441 3.6 10.4 0.5
O2P B:PEP440 3.8 13.0 0.5
CA B:THR40 3.8 27.2 1.0
O2P B:2PG441 3.9 12.2 0.5
OD1 B:ASP321 4.0 32.5 1.0
O1P B:2PG441 4.1 15.3 0.5
OD2 B:ASP321 4.1 21.0 1.0
O2 B:PEP440 4.2 15.0 0.5
NZ B:LYS345 4.2 19.6 1.0
NH2 B:ARG374 4.3 18.7 1.0
C1 B:PEP440 4.3 15.4 0.5
C B:THR40 4.3 25.3 1.0
C B:ALA38 4.4 31.6 1.0
C1 B:2PG441 4.5 15.2 0.5
CG B:ASP321 4.5 30.8 1.0
N B:GLY41 4.5 22.8 1.0
C2 B:2PG441 4.6 18.1 0.5
C2 B:PEP440 4.6 16.4 0.5
O B:ALA38 4.8 30.8 1.0
O3P B:2PG441 4.8 15.1 0.5
OD2 B:ASP320 4.8 15.1 1.0
OE2 B:GLU44 4.9 26.4 1.0
O3P B:PEP440 5.0 15.3 0.5

Reference:

P.A.Sims, A.L.Menefee, T.M.Larsen, S.O.Mansoorabadi, G.H.Reed. Structure and Catalytic Properties of An Engineered Heterodimer of Enolase Composed of One Active and One Inactive Subunit J.Mol.Biol. V. 355 422 2006.
ISSN: ISSN 0022-2836
PubMed: 16309698
DOI: 10.1016/J.JMB.2005.10.050
Page generated: Tue Aug 13 21:32:47 2024

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