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Magnesium in PDB 2xh2: Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N D321A Mutant of Yeast Enolase 1

Enzymatic activity of Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N D321A Mutant of Yeast Enolase 1

All present enzymatic activity of Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N D321A Mutant of Yeast Enolase 1:
4.2.1.11;

Protein crystallography data

The structure of Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N D321A Mutant of Yeast Enolase 1, PDB code: 2xh2 was solved by B.Schreier, B.Hocker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.65 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 64.720, 82.540, 95.610, 89.41, 71.31, 84.80
R / Rfree (%) 16.579 / 20.949

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N D321A Mutant of Yeast Enolase 1 (pdb code 2xh2). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N D321A Mutant of Yeast Enolase 1, PDB code: 2xh2:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 2xh2

Go back to Magnesium Binding Sites List in 2xh2
Magnesium binding site 1 out of 4 in the Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N D321A Mutant of Yeast Enolase 1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N D321A Mutant of Yeast Enolase 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1439

b:2.0
occ:1.00
 OE2 A:GLU295 2.0 13.1 1.0
O A:HOH2497 2.0 14.1 1.0
OD2 A:ASP246 2.1 13.9 1.0
OD2 A:ASP320 2.2 14.0 1.0
O2 A:2PG1440 2.3 14.7 1.0
O1 A:2PG1440 2.3 13.7 1.0
C1 A:2PG1440 2.6 13.7 1.0
CG A:ASP246 3.0 14.3 1.0
CD A:GLU295 3.1 12.6 1.0
CG A:ASP320 3.2 12.3 1.0
OD1 A:ASP246 3.3 13.8 1.0
CB A:ASP320 3.6 12.0 1.0
NZ A:LYS396 3.7 12.5 1.0
O A:HOH2584 3.8 34.8 1.0
OE1 A:GLU295 3.8 13.9 1.0
C2 A:2PG1440 4.1 13.2 1.0
CG A:GLU295 4.1 12.9 1.0
CD2 A:LEU343 4.2 10.9 1.0
NZ A:LYS345 4.2 14.9 1.0
O A:HOH2421 4.3 5.1 1.0
OD2 A:ASP296 4.3 11.6 1.0
CB A:ASP246 4.3 13.8 1.0
OD1 A:ASP320 4.3 9.7 1.0
O A:HOH2418 4.4 25.1 1.0
O1P A:2PG1440 4.8 14.2 1.0
CG A:ASP296 4.9 11.7 1.0
C3 A:2PG1440 4.9 14.5 1.0
O3 A:2PG1440 4.9 15.8 1.0

Magnesium binding site 2 out of 4 in 2xh2

Go back to Magnesium Binding Sites List in 2xh2
Magnesium binding site 2 out of 4 in the Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N D321A Mutant of Yeast Enolase 1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N D321A Mutant of Yeast Enolase 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1439

b:2.0
occ:1.00
 O B:HOH2625 2.1 13.4 1.0
OE2 B:GLU295 2.1 12.9 1.0
O B:HOH2618 2.1 15.3 1.0
OD2 B:ASP320 2.2 16.3 1.0
OD2 B:ASP246 2.2 14.1 1.0
O B:HOH2487 2.2 12.1 1.0
CG B:ASP246 3.1 14.9 1.0
CG B:ASP320 3.2 16.2 1.0
CD B:GLU295 3.3 12.8 1.0
OD1 B:ASP246 3.4 14.0 1.0
CB B:ASP320 3.7 14.0 1.0
O1 B:2PG1440 3.9 18.9 1.0
NE2 B:GLN167 4.0 16.0 1.0
OE1 B:GLU295 4.1 14.6 1.0
O2 B:2PG1440 4.2 18.7 1.0
O B:HOH2188 4.2 25.6 1.0
OE2 B:GLU168 4.2 15.0 1.0
CG B:GLU295 4.3 13.0 1.0
NZ B:LYS396 4.3 9.4 1.0
OD1 B:ASP320 4.3 16.6 1.0
OD2 B:ASP296 4.4 14.7 1.0
CB B:ASP246 4.4 14.1 1.0
O B:HOH2513 4.4 37.7 1.0
C1 B:2PG1440 4.4 18.8 1.0
CD2 B:LEU343 4.5 11.8 1.0
CD B:GLU168 4.8 15.5 1.0
NZ B:LYS345 4.8 13.2 1.0
CB B:ALA248 4.9 15.2 1.0
OE1 B:GLU168 5.0 14.4 1.0

Magnesium binding site 3 out of 4 in 2xh2

Go back to Magnesium Binding Sites List in 2xh2
Magnesium binding site 3 out of 4 in the Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N D321A Mutant of Yeast Enolase 1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N D321A Mutant of Yeast Enolase 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1439

b:5.2
occ:1.00
 OE2 C:GLU295 2.0 13.1 1.0
OD2 C:ASP320 2.1 15.1 1.0
O C:HOH2446 2.2 16.2 1.0
OD2 C:ASP246 2.2 16.5 1.0
O1 C:2PG1440 2.3 16.7 1.0
O2 C:2PG1440 2.4 18.4 1.0
C1 C:2PG1440 2.7 15.8 1.0
CG C:ASP246 3.1 16.1 1.0
CD C:GLU295 3.2 13.6 1.0
CG C:ASP320 3.2 15.5 1.0
OD1 C:ASP246 3.3 15.2 1.0
CB C:ASP320 3.6 12.9 1.0
NZ C:LYS396 3.8 16.8 1.0
O C:HOH2519 3.8 39.9 1.0
OE1 C:GLU295 3.8 12.4 1.0
C2 C:2PG1440 4.2 15.9 1.0
CG C:GLU295 4.2 14.4 1.0
CD2 C:LEU343 4.2 11.1 1.0
NZ C:LYS345 4.2 12.8 1.0
OD2 C:ASP296 4.2 17.0 1.0
OD1 C:ASP320 4.3 14.1 1.0
CB C:ASP246 4.4 16.2 1.0
O C:HOH2384 4.4 9.9 1.0
O C:HOH2383 4.5 29.1 1.0
O1P C:2PG1440 4.8 15.0 1.0
CE C:LYS345 4.9 12.5 1.0
CE C:LYS396 4.9 15.5 1.0
O3 C:2PG1440 4.9 18.5 1.0
CG C:ASP296 5.0 16.1 1.0

Magnesium binding site 4 out of 4 in 2xh2

Go back to Magnesium Binding Sites List in 2xh2
Magnesium binding site 4 out of 4 in the Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N D321A Mutant of Yeast Enolase 1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N D321A Mutant of Yeast Enolase 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1439

b:2.0
occ:1.00
 OE2 D:GLU295 2.0 15.2 1.0
O D:HOH2619 2.1 15.2 1.0
O D:HOH2446 2.1 13.3 1.0
O D:HOH2620 2.2 15.9 1.0
OD2 D:ASP320 2.2 12.2 1.0
OD2 D:ASP246 2.2 13.4 1.0
CG D:ASP246 3.0 14.6 1.0
CD D:GLU295 3.2 14.9 1.0
CG D:ASP320 3.2 14.6 1.0
OD1 D:ASP246 3.3 12.1 1.0
CB D:ASP320 3.7 13.9 1.0
O1 D:2PG1440 3.9 18.0 1.0
OE1 D:GLU295 4.1 16.6 1.0
CG D:GLU295 4.1 13.7 1.0
OE2 D:GLU168 4.3 18.7 1.0
O D:HOH2516 4.3 32.6 1.0
NZ D:LYS396 4.3 11.3 1.0
O2 D:2PG1440 4.3 17.8 1.0
CB D:ASP246 4.3 13.5 1.0
O D:HOH2179 4.3 21.5 1.0
OD1 D:ASP320 4.3 14.2 1.0
OD2 D:ASP296 4.3 15.3 1.0
OE1 D:GLN167 4.4 17.7 1.0
CD2 D:LEU343 4.5 11.0 1.0
C1 D:2PG1440 4.5 18.1 1.0
CD D:GLU168 4.8 15.7 1.0
NZ D:LYS345 4.9 11.1 1.0
O D:HOH2560 5.0 13.6 1.0
CB D:ALA248 5.0 17.2 1.0

Reference:

B.Schreier, B.Hoecker. Engineering the Enolase Magnesium II Binding Site - Implications For Its Evolution. Biochemistry V. 49 7582 2010.
ISSN: ISSN 0006-2960
PubMed: 20690637
DOI: 10.1021/BI100954F
Page generated: Wed Aug 14 07:07:23 2024

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