Atomistry » Magnesium » PDB 2xbp-2xnd » 2xh2
Atomistry »
  Magnesium »
    PDB 2xbp-2xnd »
      2xh2 »

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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy