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Magnesium in PDB 2xh0: Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N Q167K D321R Mutant of Yeast Enolase 1

Enzymatic activity of Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N Q167K D321R Mutant of Yeast Enolase 1

All present enzymatic activity of Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N Q167K D321R 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 Q167K D321R Mutant of Yeast Enolase 1, PDB code: 2xh0 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) 37.85 / 1.70
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 55.329, 60.797, 120.667, 89.89, 89.90, 65.84
R / Rfree (%) 19.7 / 24.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N Q167K D321R Mutant of Yeast Enolase 1 (pdb code 2xh0). 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 Q167K D321R Mutant of Yeast Enolase 1, PDB code: 2xh0:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 2xh0

Go back to Magnesium Binding Sites List in 2xh0
Magnesium binding site 1 out of 4 in the Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N Q167K D321R 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 Q167K D321R Mutant of Yeast Enolase 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1439

b:2.0
occ:1.00
 OD2 A:ASP320 2.0 12.2 1.0
O A:HOH2302 2.1 16.2 1.0
OE2 A:GLU295 2.1 12.4 1.0
O2' A:PEP1440 2.2 16.6 1.0
OD2 A:ASP246 2.4 15.3 1.0
O1 A:PEP1440 2.4 14.0 1.0
C1 A:PEP1440 2.6 15.6 1.0
CG A:ASP320 3.1 11.0 1.0
CG A:ASP246 3.1 13.5 1.0
CD A:GLU295 3.3 12.3 1.0
OD1 A:ASP246 3.3 11.4 1.0
CB A:ASP320 3.7 9.6 1.0
NH1 A:ARG321 3.7 21.3 1.0
NZ A:LYS396 3.9 10.4 1.0
NZ A:LYS345 3.9 11.6 1.0
OE1 A:GLU295 4.0 11.6 1.0
C2 A:PEP1440 4.1 13.6 1.0
OD2 A:ASP296 4.2 14.8 1.0
OD1 A:ASP320 4.2 9.9 1.0
CG A:GLU295 4.2 11.2 1.0
CD2 A:LEU343 4.3 8.3 1.0
NZ A:LYS167 4.3 24.5 1.0
CB A:ASP246 4.5 12.0 1.0
CE A:LYS167 4.7 22.2 1.0
CG A:ASP296 4.9 11.7 1.0
O2 A:PEP1440 4.9 13.1 1.0
CZ A:ARG321 4.9 18.6 1.0

Magnesium binding site 2 out of 4 in 2xh0

Go back to Magnesium Binding Sites List in 2xh0
Magnesium binding site 2 out of 4 in the Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N Q167K D321R 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 Q167K D321R Mutant of Yeast Enolase 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1439

b:2.7
occ:1.00
 O B:HOH2277 2.0 13.8 1.0
OD2 B:ASP320 2.0 12.9 1.0
OE2 B:GLU295 2.3 15.3 1.0
O2' B:PEP1440 2.3 18.0 1.0
OD2 B:ASP246 2.3 15.1 1.0
O1 B:PEP1440 2.4 15.2 1.0
C1 B:PEP1440 2.7 17.8 1.0
CG B:ASP246 3.1 12.7 1.0
CG B:ASP320 3.2 11.6 1.0
OD1 B:ASP246 3.2 13.2 1.0
CD B:GLU295 3.4 13.6 1.0
O B:HOH2321 3.6 32.5 1.0
CB B:ASP320 3.7 10.4 1.0
NH1 B:ARG321 3.9 22.7 1.0
NZ B:LYS345 4.0 12.7 1.0
OE1 B:GLU295 4.2 13.8 1.0
C2 B:PEP1440 4.2 15.5 1.0
NZ B:LYS396 4.2 13.7 1.0
OD1 B:ASP320 4.2 11.5 1.0
OD2 B:ASP296 4.2 13.6 1.0
CG B:GLU295 4.3 11.8 1.0
CD2 B:LEU343 4.4 11.3 1.0
NZ B:LYS167 4.4 25.6 1.0
CB B:ASP246 4.5 11.6 1.0
CE B:LYS167 4.6 23.3 1.0
OE2 B:GLU168 4.8 18.2 1.0
CG B:ASP296 4.9 11.5 1.0
O2 B:PEP1440 4.9 14.1 1.0
CZ B:ARG321 5.0 22.3 1.0

Magnesium binding site 3 out of 4 in 2xh0

Go back to Magnesium Binding Sites List in 2xh0
Magnesium binding site 3 out of 4 in the Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N Q167K D321R 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 Q167K D321R Mutant of Yeast Enolase 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1439

b:2.0
occ:1.00
 OD2 C:ASP320 2.0 9.8 1.0
O C:HOH2271 2.0 8.4 1.0
OE2 C:GLU295 2.1 10.4 1.0
O2' C:PEP1440 2.2 14.6 1.0
OD2 C:ASP246 2.3 19.4 1.0
O1 C:PEP1440 2.5 14.9 1.0
C1 C:PEP1440 2.6 15.2 1.0
CG C:ASP320 3.1 7.6 1.0
CG C:ASP246 3.2 12.4 1.0
CD C:GLU295 3.2 9.8 1.0
OD1 C:ASP246 3.4 11.4 1.0
NH1 C:ARG321 3.6 19.4 1.0
CB C:ASP320 3.7 9.1 1.0
NZ C:LYS345 3.9 13.4 1.0
NZ C:LYS396 3.9 8.6 1.0
OE1 C:GLU295 4.0 9.8 1.0
CG C:GLU295 4.1 9.2 1.0
C2 C:PEP1440 4.1 13.0 1.0
OD1 C:ASP320 4.1 9.0 1.0
OD2 C:ASP296 4.3 12.8 1.0
CD2 C:LEU343 4.4 8.5 1.0
NZ C:LYS167 4.4 24.8 1.0
CB C:ASP246 4.5 11.0 1.0
CZ C:ARG321 4.7 17.7 1.0
O2 C:PEP1440 4.8 11.2 1.0
CE C:LYS167 4.8 21.3 1.0
CG C:ASP296 4.9 9.7 1.0

Magnesium binding site 4 out of 4 in 2xh0

Go back to Magnesium Binding Sites List in 2xh0
Magnesium binding site 4 out of 4 in the Engineering the Enolase Active Site Pocket: Crystal Structure of the S39N Q167K D321R 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 Q167K D321R Mutant of Yeast Enolase 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1439

b:2.2
occ:1.00
 O D:HOH2192 2.0 13.9 1.0
OD2 D:ASP320 2.1 10.4 1.0
OE2 D:GLU295 2.1 12.2 1.0
OD2 D:ASP246 2.3 14.5 1.0
O2' D:PEP1440 2.3 23.7 1.0
O1 D:PEP1440 2.4 21.2 1.0
C1 D:PEP1440 2.7 22.3 1.0
CG D:ASP246 3.1 12.9 1.0
OD1 D:ASP246 3.2 13.1 1.0
CG D:ASP320 3.2 9.0 1.0
CD D:GLU295 3.3 10.6 1.0
CB D:ASP320 3.7 9.9 1.0
O D:HOH2228 3.8 37.0 1.0
NH1 D:ARG321 3.8 23.0 1.0
NZ D:LYS396 3.9 15.4 1.0
OE1 D:GLU295 4.1 10.2 1.0
NZ D:LYS345 4.1 12.5 1.0
C2 D:PEP1440 4.2 20.4 1.0
OD1 D:ASP320 4.2 9.8 1.0
CG D:GLU295 4.2 8.9 1.0
OD2 D:ASP296 4.3 11.2 1.0
CD2 D:LEU343 4.3 7.1 1.0
NZ D:LYS167 4.4 22.9 1.0
CB D:ASP246 4.4 11.8 1.0
CE D:LYS167 4.6 21.6 1.0
OE2 D:GLU168 4.8 20.5 1.0
O2 D:PEP1440 4.9 18.1 1.0
CG D:ASP296 4.9 10.6 1.0
CZ D:ARG321 4.9 21.9 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 07:07:12 2024

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