Atomistry » Magnesium » PDB 3t2d-3tar » 3t2q
Atomistry »
  Magnesium »
    PDB 3t2d-3tar »
      3t2q »

Magnesium in PDB 3t2q: E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone

Enzymatic activity of E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone

All present enzymatic activity of E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone:
3.2.1.23;

Protein crystallography data

The structure of E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone, PDB code: 3t2q was solved by L.J.Jancewicz, R.W.Wheatley, G.Sutendra, M.Lee, M.Fraser, R.E.Huber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 80.00 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 152.270, 163.540, 203.740, 90.00, 90.00, 90.00
R / Rfree (%) 18 / 23.9

Other elements in 3t2q:

The structure of E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone also contains other interesting chemical elements:

Sodium (Na) 11 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone (pdb code 3t2q). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 8 binding sites of Magnesium where determined in the E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone, PDB code: 3t2q:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Magnesium binding site 1 out of 8 in 3t2q

Go back to Magnesium Binding Sites List in 3t2q
Magnesium binding site 1 out of 8 in the E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg3001

b:43.2
occ:1.00
 O A:HOH4549 2.0 50.0 1.0
ND1 A:HIS418 2.0 40.4 1.0
OE2 A:GLU416 2.1 39.5 1.0
OE1 A:GLU461 2.1 43.4 1.0
O A:HOH4101 2.1 38.3 1.0
O A:HOH4537 2.2 30.6 1.0
CE1 A:HIS418 2.9 40.6 1.0
CD A:GLU461 3.1 41.9 1.0
CG A:HIS418 3.1 35.3 1.0
CD A:GLU416 3.3 36.1 1.0
CB A:HIS418 3.6 32.1 1.0
OE2 A:GLU461 3.7 40.0 1.0
OE1 A:GLU416 3.8 34.9 1.0
C2 A:1492001 4.0 84.3 1.0
NE2 A:HIS418 4.1 37.3 1.0
CG A:GLU461 4.1 39.0 1.0
CB A:GLU461 4.1 27.9 1.0
OD1 A:ASN102 4.2 52.9 1.0
CD2 A:HIS418 4.2 31.8 1.0
ND2 A:ASN460 4.2 26.4 1.0
O3 A:1492001 4.3 71.0 1.0
N A:ASP201 4.3 45.9 1.0
CB A:ASP201 4.4 47.8 1.0
O A:ASP199 4.4 39.4 1.0
CG A:GLU416 4.4 33.7 1.0
O4 A:1492001 4.4 81.7 1.0
O2 A:1492001 4.5 74.3 1.0
O A:ASN102 4.7 50.7 1.0
C3 A:1492001 4.7 81.5 1.0
C1 A:1492001 4.9 87.2 1.0
CA A:ASP201 4.9 46.6 1.0
CG2 A:VAL103 5.0 45.6 1.0

Magnesium binding site 2 out of 8 in 3t2q

Go back to Magnesium Binding Sites List in 3t2q
Magnesium binding site 2 out of 8 in the E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg3002

b:44.1
occ:1.00
 OD2 A:ASP193 2.1 53.1 1.0
O A:ASP15 2.1 49.7 1.0
O A:ASN18 2.3 45.7 1.0
OE1 A:GLN163 2.3 44.6 1.0
O A:VAL21 2.3 41.2 1.0
CG A:ASP193 3.0 50.1 1.0
CD A:GLN163 3.1 40.6 1.0
OD1 A:ASP193 3.2 47.4 1.0
C A:ASN18 3.2 49.4 1.0
C A:ASP15 3.3 51.1 1.0
NE2 A:GLN163 3.4 38.1 1.0
C A:VAL21 3.5 39.2 1.0
N A:ASN18 3.7 53.6 1.0
OH A:TYR161 3.8 47.1 1.0
CA A:TRP16 3.9 47.8 1.0
CA A:ASN18 3.9 54.5 1.0
N A:TRP16 4.0 51.3 1.0
N A:PRO19 4.2 50.0 1.0
C A:TRP16 4.2 47.6 1.0
CE2 A:TYR161 4.3 41.0 1.0
CB A:ASN18 4.3 56.2 1.0
CA A:VAL21 4.3 40.1 1.0
CB A:ASP193 4.4 42.2 1.0
CG A:GLN163 4.4 36.6 1.0
CA A:PRO19 4.4 48.5 1.0
N A:VAL21 4.4 41.9 1.0
CA A:ASP15 4.5 52.9 1.0
N A:THR22 4.5 38.7 1.0
N A:GLU17 4.5 47.5 1.0
CB A:VAL21 4.5 47.2 1.0
CZ A:TYR161 4.5 42.5 1.0
CA A:THR22 4.6 40.0 1.0
CG1 A:VAL21 4.7 38.7 1.0
O A:TRP16 4.8 44.4 1.0
CB A:ASP15 4.8 51.6 1.0
C A:GLU17 4.9 52.0 1.0
C A:PRO19 4.9 49.3 1.0

Magnesium binding site 3 out of 8 in 3t2q

Go back to Magnesium Binding Sites List in 3t2q
Magnesium binding site 3 out of 8 in the E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg3001

b:41.1
occ:1.00
 OE1 B:GLU461 2.1 43.9 1.0
OE2 B:GLU416 2.1 29.0 1.0
O B:HOH4514 2.2 33.3 1.0
O B:HOH4065 2.3 34.7 1.0
O B:HOH4118 2.4 38.6 1.0
ND1 B:HIS418 2.5 37.9 1.0
CD B:GLU416 3.2 26.8 1.0
CD B:GLU461 3.2 39.3 1.0
CE1 B:HIS418 3.4 33.0 1.0
CG B:HIS418 3.5 35.9 1.0
OE1 B:GLU416 3.6 33.4 1.0
CB B:HIS418 3.8 29.2 1.0
OE2 B:GLU461 3.8 43.5 1.0
OD1 B:ASN102 4.0 50.2 1.0
CB B:ASP201 4.0 40.3 1.0
C2 B:1492001 4.0 58.8 1.0
N B:ASP201 4.1 40.0 1.0
O4 B:1492001 4.1 57.1 1.0
O B:ASP199 4.2 39.3 1.0
ND2 B:ASN460 4.3 25.1 1.0
O3 B:1492001 4.4 43.3 1.0
CG B:GLU461 4.4 36.3 1.0
O2 B:1492001 4.4 52.1 1.0
CB B:GLU461 4.4 28.8 1.0
CG B:GLU416 4.4 27.9 1.0
O B:ASN102 4.5 48.7 1.0
NE2 B:HIS418 4.6 35.2 1.0
CD2 B:HIS418 4.6 29.2 1.0
CA B:ASP201 4.7 40.7 1.0
C3 B:1492001 4.7 58.1 1.0
C B:GLN200 4.9 40.1 1.0
CA B:GLN200 5.0 36.1 1.0

Magnesium binding site 4 out of 8 in 3t2q

Go back to Magnesium Binding Sites List in 3t2q
Magnesium binding site 4 out of 8 in the E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg3002

b:38.5
occ:1.00
 OD2 B:ASP193 2.1 49.5 1.0
O B:ASP15 2.1 44.1 1.0
O B:ASN18 2.3 38.9 1.0
OE1 B:GLN163 2.3 41.9 1.0
O B:VAL21 2.3 39.7 1.0
CG B:ASP193 2.9 45.5 1.0
OD1 B:ASP193 3.1 48.5 1.0
C B:ASN18 3.2 44.3 1.0
CD B:GLN163 3.2 45.5 1.0
C B:ASP15 3.3 43.8 1.0
C B:VAL21 3.5 41.6 1.0
N B:ASN18 3.5 43.8 1.0
NE2 B:GLN163 3.6 37.9 1.0
CA B:ASN18 3.8 44.7 1.0
CA B:TRP16 4.0 46.4 1.0
OH B:TYR161 4.0 41.0 1.0
N B:TRP16 4.1 44.8 1.0
N B:PRO19 4.1 46.8 1.0
C B:TRP16 4.2 45.3 1.0
CA B:VAL21 4.3 43.7 1.0
CB B:ASN18 4.3 41.5 1.0
N B:GLU17 4.3 44.2 1.0
N B:VAL21 4.4 45.9 1.0
CB B:ASP193 4.4 37.2 1.0
CB B:VAL21 4.4 47.6 1.0
CE2 B:TYR161 4.4 35.8 1.0
CA B:PRO19 4.4 47.3 1.0
CA B:ASP15 4.4 47.0 1.0
N B:THR22 4.5 39.5 1.0
CG B:GLN163 4.6 38.5 1.0
CA B:THR22 4.7 42.3 1.0
CZ B:TYR161 4.7 42.5 1.0
C B:GLU17 4.7 43.3 1.0
O B:TRP16 4.8 46.4 1.0
CG1 B:VAL21 4.8 48.7 1.0
C B:PRO19 4.9 45.4 1.0
CB B:ASP15 4.9 46.4 1.0

Magnesium binding site 5 out of 8 in 3t2q

Go back to Magnesium Binding Sites List in 3t2q
Magnesium binding site 5 out of 8 in the E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg3001

b:44.9
occ:1.00
 ND1 C:HIS418 2.1 42.3 1.0
OE1 C:GLU461 2.1 36.6 1.0
OE2 C:GLU416 2.1 35.8 1.0
O C:HOH4124 2.2 37.7 1.0
O C:HOH4045 2.2 41.7 1.0
O C:HOH4523 2.2 36.8 1.0
CE1 C:HIS418 2.9 28.4 1.0
CD C:GLU461 3.2 32.6 1.0
CG C:HIS418 3.2 36.9 1.0
CD C:GLU416 3.3 37.3 1.0
CB C:HIS418 3.6 30.6 1.0
OD1 C:ASN102 3.8 47.9 1.0
OE2 C:GLU461 3.8 38.4 1.0
OE1 C:GLU416 3.9 36.3 1.0
NE2 C:HIS418 4.1 32.8 1.0
C2 C:1492001 4.1 67.0 1.0
CB C:GLU461 4.2 26.0 1.0
CG C:GLU461 4.2 27.9 1.0
CD2 C:HIS418 4.2 32.9 1.0
CB C:ASP201 4.3 42.1 1.0
O C:ASP199 4.3 30.2 1.0
N C:ASP201 4.3 36.9 1.0
O2 C:1492001 4.3 59.6 1.0
CG C:GLU416 4.4 34.5 1.0
O4 C:1492001 4.4 63.2 1.0
ND2 C:ASN460 4.5 26.3 1.0
O3 C:1492001 4.5 57.4 1.0
O C:ASN102 4.6 48.7 1.0
CA C:ASP201 4.8 42.0 1.0
C3 C:1492001 4.8 65.4 1.0

Magnesium binding site 6 out of 8 in 3t2q

Go back to Magnesium Binding Sites List in 3t2q
Magnesium binding site 6 out of 8 in the E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg3002

b:43.4
occ:1.00
 OD2 C:ASP193 2.1 45.6 1.0
O C:ASP15 2.1 44.2 1.0
OE1 C:GLN163 2.2 37.4 1.0
O C:ASN18 2.3 47.5 1.0
O C:VAL21 2.3 39.9 1.0
CG C:ASP193 2.9 40.7 1.0
OD1 C:ASP193 3.0 50.3 1.0
C C:ASN18 3.2 50.0 1.0
CD C:GLN163 3.2 33.5 1.0
C C:ASP15 3.3 47.7 1.0
C C:VAL21 3.5 39.7 1.0
NE2 C:GLN163 3.6 29.2 1.0
N C:ASN18 3.6 52.9 1.0
CA C:ASN18 3.9 51.7 1.0
CA C:TRP16 4.0 47.2 1.0
OH C:TYR161 4.0 34.7 1.0
N C:TRP16 4.1 45.5 1.0
C C:TRP16 4.2 48.5 1.0
N C:PRO19 4.2 47.1 1.0
CA C:VAL21 4.3 42.5 1.0
CB C:ASP193 4.3 35.1 1.0
N C:GLU17 4.3 49.5 1.0
CB C:ASN18 4.3 51.6 1.0
CB C:VAL21 4.4 41.5 1.0
N C:VAL21 4.4 46.3 1.0
CA C:PRO19 4.4 45.4 1.0
CA C:ASP15 4.4 48.8 1.0
N C:THR22 4.5 40.3 1.0
CE2 C:TYR161 4.5 30.6 1.0
CG C:GLN163 4.6 34.5 1.0
CA C:THR22 4.7 39.8 1.0
O C:TRP16 4.7 48.4 1.0
CZ C:TYR161 4.7 35.4 1.0
CG1 C:VAL21 4.8 37.3 1.0
C C:GLU17 4.8 51.9 1.0
CB C:ASP15 4.9 41.2 1.0
C C:PRO19 4.9 45.5 1.0

Magnesium binding site 7 out of 8 in 3t2q

Go back to Magnesium Binding Sites List in 3t2q
Magnesium binding site 7 out of 8 in the E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg3001

b:43.6
occ:1.00
 ND1 D:HIS418 2.1 43.1 1.0
OE1 D:GLU461 2.1 34.5 1.0
O D:HOH4469 2.1 51.5 1.0
OE2 D:GLU416 2.1 42.2 1.0
O D:HOH4461 2.1 37.7 1.0
O D:HOH4034 2.2 36.1 1.0
CE1 D:HIS418 2.9 40.2 1.0
CD D:GLU461 3.1 43.0 1.0
CG D:HIS418 3.1 38.6 1.0
CD D:GLU416 3.3 36.6 1.0
CB D:HIS418 3.6 34.1 1.0
OE2 D:GLU461 3.7 42.2 1.0
OE1 D:GLU416 3.8 41.3 1.0
C2 D:1492001 4.0 82.9 1.0
CB D:GLU461 4.0 31.6 1.0
NE2 D:HIS418 4.1 40.0 1.0
CG D:GLU461 4.1 35.1 1.0
OD1 D:ASN102 4.1 58.2 1.0
CD2 D:HIS418 4.2 32.6 1.0
N D:ASP201 4.3 49.8 1.0
ND2 D:ASN460 4.3 35.5 1.0
CB D:ASP201 4.3 57.9 1.0
O3 D:1492001 4.3 70.0 1.0
O D:ASP199 4.3 42.4 1.0
O4 D:1492001 4.4 65.7 1.0
CG D:GLU416 4.4 35.0 1.0
O2 D:1492001 4.5 70.9 1.0
O D:ASN102 4.6 57.3 1.0
C3 D:1492001 4.7 76.3 1.0
C1 D:1492001 4.8 85.9 1.0
CA D:ASP201 4.9 53.4 1.0
CA D:HIS418 5.0 33.6 1.0

Magnesium binding site 8 out of 8 in 3t2q

Go back to Magnesium Binding Sites List in 3t2q
Magnesium binding site 8 out of 8 in the E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of E. Coli (Lacz) Beta-Galactosidase (S796D) in Complex with Galactonolactone within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg3002

b:51.2
occ:1.00
 OD2 D:ASP193 2.1 41.7 1.0
O D:ASP15 2.1 52.2 1.0
O D:ASN18 2.3 48.8 1.0
OE1 D:GLN163 2.3 53.7 1.0
O D:VAL21 2.3 48.2 1.0
CG D:ASP193 2.9 50.2 1.0
OD1 D:ASP193 3.0 51.8 1.0
CD D:GLN163 3.2 42.9 1.0
C D:ASN18 3.2 53.0 1.0
C D:ASP15 3.3 52.3 1.0
C D:VAL21 3.5 42.0 1.0
NE2 D:GLN163 3.5 44.9 1.0
N D:ASN18 3.7 56.6 1.0
CA D:TRP16 3.9 52.8 1.0
CA D:ASN18 4.0 54.4 1.0
N D:TRP16 4.0 52.3 1.0
OH D:TYR161 4.1 33.7 1.0
C D:TRP16 4.2 52.4 1.0
N D:PRO19 4.2 50.9 1.0
CA D:VAL21 4.2 41.7 1.0
CB D:VAL21 4.3 45.9 1.0
N D:VAL21 4.3 44.4 1.0
CB D:ASP193 4.3 43.8 1.0
N D:GLU17 4.4 53.5 1.0
CA D:PRO19 4.4 50.4 1.0
CA D:ASP15 4.4 52.8 1.0
CB D:ASN18 4.4 55.3 1.0
CE2 D:TYR161 4.5 34.7 1.0
N D:THR22 4.5 38.0 1.0
CG D:GLN163 4.5 34.7 1.0
CA D:THR22 4.7 39.1 1.0
O D:TRP16 4.7 49.2 1.0
CZ D:TYR161 4.7 37.0 1.0
CG1 D:VAL21 4.8 35.0 1.0
C D:PRO19 4.8 50.2 1.0
CB D:ASP15 4.9 49.2 1.0
C D:GLU17 4.9 56.3 1.0

Reference:

L.J.Jancewicz, R.W.Wheatley, G.Sutendra, M.Lee, M.E.Fraser, R.E.Huber. Ser-796 of Beta-Galactosidase (E. Coli) Plays A Key Role in Maintaining An Optimum Balance Between the Opened and Closed Conformations of the Catalytically Important Active Site Loop Arch.Biochem.Biophys. V. 517 111 2012.
ISSN: ISSN 0003-9861
PubMed: 22155115
DOI: 10.1016/J.ABB.2011.11.017
Page generated: Thu Aug 15 11:50:36 2024

Last articles

F in 8Q10
F in 8Q0X
F in 8Q0W
F in 8Q11
F in 8Q0C
F in 8PTG
F in 8Q0V
F in 8PYW
F in 8PWM
F in 8PY3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy