Atomistry » Magnesium » PDB 1pi3-1q24 » 1px3
Atomistry »
  Magnesium »
    PDB 1pi3-1q24 »
      1px3 »

Magnesium in PDB 1px3: E. Coli (Lacz) Beta-Galactosidase (G794A)

Enzymatic activity of E. Coli (Lacz) Beta-Galactosidase (G794A)

All present enzymatic activity of E. Coli (Lacz) Beta-Galactosidase (G794A):
3.2.1.23;

Protein crystallography data

The structure of E. Coli (Lacz) Beta-Galactosidase (G794A), PDB code: 1px3 was solved by D.H.Juers, S.Hakda, B.W.Matthews, R.E.Huber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 21.70 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 149.700, 168.590, 200.990, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1px3:

The structure of E. Coli (Lacz) Beta-Galactosidase (G794A) also contains other interesting chemical elements:

Sodium (Na) 16 atoms

Magnesium Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Magnesium atom in the E. Coli (Lacz) Beta-Galactosidase (G794A) (pdb code 1px3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 12 binding sites of Magnesium where determined in the E. Coli (Lacz) Beta-Galactosidase (G794A), PDB code: 1px3:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 12 in 1px3

Go back to Magnesium Binding Sites List in 1px3
Magnesium binding site 1 out of 12 in the E. Coli (Lacz) Beta-Galactosidase (G794A)


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 (G794A) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg3001

b:17.6
occ:1.00
 O A:HOH8680 2.0 11.1 1.0
O A:HOH8616 2.1 13.3 1.0
O A:HOH8756 2.1 13.1 1.0
OE2 A:GLU416 2.1 15.4 1.0
OE1 A:GLU461 2.2 18.1 1.0
ND1 A:HIS418 2.3 13.8 1.0
CE1 A:HIS418 3.1 17.7 1.0
CD A:GLU461 3.2 23.4 1.0
CD A:GLU416 3.3 17.8 1.0
CG A:HIS418 3.4 18.5 1.0
OE1 A:GLU416 3.7 14.0 1.0
CB A:HIS418 3.7 11.4 1.0
OE2 A:GLU461 4.0 19.4 1.0
OD1 A:ASN102 4.1 20.4 1.0
CB A:GLU461 4.1 9.7 1.0
CB A:ASP201 4.2 12.9 1.0
CG A:GLU461 4.2 10.7 1.0
N A:ASP201 4.2 14.8 1.0
O A:HOH8603 4.3 18.9 1.0
O A:ASP199 4.3 15.6 1.0
ND2 A:ASN460 4.3 13.3 1.0
NE2 A:HIS418 4.3 16.4 1.0
CG A:GLU416 4.4 8.6 1.0
CD2 A:HIS418 4.5 17.2 1.0
O A:ASN102 4.6 19.5 1.0
O A:HOH8891 4.6 21.5 1.0
CA A:ASP201 4.8 14.5 1.0
CA A:GLN200 4.9 10.5 1.0
C A:GLN200 4.9 15.9 1.0

Magnesium binding site 2 out of 12 in 1px3

Go back to Magnesium Binding Sites List in 1px3
Magnesium binding site 2 out of 12 in the E. Coli (Lacz) Beta-Galactosidase (G794A)


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 (G794A) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg3002

b:17.5
occ:1.00
 O A:ASN18 2.2 17.3 1.0
O A:ASP15 2.2 19.0 1.0
OE1 A:GLN163 2.3 16.2 1.0
O A:VAL21 2.3 16.4 1.0
OD2 A:ASP193 2.4 17.9 1.0
CG A:ASP193 3.1 25.1 1.0
OD1 A:ASP193 3.1 19.4 1.0
C A:ASN18 3.1 16.8 1.0
CD A:GLN163 3.2 16.9 1.0
C A:ASP15 3.4 21.1 1.0
C A:VAL21 3.5 18.5 1.0
NE2 A:GLN163 3.5 16.6 1.0
N A:ASN18 3.6 22.2 1.0
CA A:ASN18 3.8 19.5 1.0
OH A:TYR161 4.0 13.7 1.0
CA A:TRP16 4.0 16.0 1.0
N A:PRO19 4.1 19.3 1.0
CB A:ASN18 4.1 16.8 1.0
N A:TRP16 4.1 18.2 1.0
C A:TRP16 4.2 19.2 1.0
CA A:VAL21 4.2 12.2 1.0
N A:VAL21 4.2 14.3 1.0
CB A:VAL21 4.3 17.6 1.0
CE2 A:TYR161 4.4 15.3 1.0
CA A:PRO19 4.4 14.2 1.0
N A:GLU17 4.4 17.6 1.0
CA A:ASP15 4.5 16.6 1.0
CG A:GLN163 4.5 16.3 1.0
CB A:ASP193 4.5 14.2 1.0
N A:THR22 4.5 15.2 1.0
CZ A:TYR161 4.7 13.5 1.0
CA A:THR22 4.7 20.9 1.0
O A:TRP16 4.7 19.2 1.0
C A:GLU17 4.8 27.1 1.0
C A:PRO19 4.8 16.6 1.0
CG1 A:VAL21 4.8 18.5 1.0
CB A:ASP15 4.9 17.6 1.0
CG A:ASN18 5.0 20.7 1.0

Magnesium binding site 3 out of 12 in 1px3

Go back to Magnesium Binding Sites List in 1px3
Magnesium binding site 3 out of 12 in the E. Coli (Lacz) Beta-Galactosidase (G794A)


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 (G794A) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg3005

b:42.2
occ:1.00
 O A:HOH9343 1.8 29.4 1.0
O A:HOH9344 1.9 41.8 1.0
O A:HOH9399 2.3 31.8 1.0
O A:HOH9192 2.3 29.6 1.0
C1 A:DMS8406 3.4 59.8 1.0
O A:DMS8406 4.0 45.9 1.0
OE2 A:GLU314 4.0 21.4 1.0
OE1 A:GLU314 4.2 17.4 1.0
S A:DMS8406 4.3 77.7 1.0
O A:HOH9421 4.3 41.0 1.0
O A:HOH9234 4.6 22.2 1.0
CD A:GLU314 4.6 19.5 1.0

Magnesium binding site 4 out of 12 in 1px3

Go back to Magnesium Binding Sites List in 1px3
Magnesium binding site 4 out of 12 in the E. Coli (Lacz) Beta-Galactosidase (G794A)


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 (G794A) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg3001

b:14.2
occ:1.00
 O B:HOH8694 2.0 11.9 1.0
OE1 B:GLU461 2.0 14.3 1.0
O B:HOH8771 2.1 12.5 1.0
OE2 B:GLU416 2.1 13.0 1.0
ND1 B:HIS418 2.1 13.6 1.0
O B:HOH8630 2.2 11.1 1.0
CD B:GLU461 3.0 13.7 1.0
CE1 B:HIS418 3.0 12.9 1.0
CG B:HIS418 3.3 14.9 1.0
CD B:GLU416 3.3 13.1 1.0
CB B:HIS418 3.6 11.3 1.0
OE1 B:GLU416 3.7 13.7 1.0
O B:HOH9142 3.7 44.5 1.0
OE2 B:GLU461 3.8 15.4 1.0
CB B:GLU461 4.0 10.4 1.0
OD1 B:ASN102 4.0 17.2 1.0
CG B:GLU461 4.1 8.9 1.0
CB B:ASP201 4.2 15.6 1.0
O B:HOH8617 4.2 24.8 1.0
N B:ASP201 4.2 13.4 1.0
NE2 B:HIS418 4.3 12.3 1.0
ND2 B:ASN460 4.3 12.7 1.0
CD2 B:HIS418 4.4 14.0 1.0
O B:ASP199 4.4 13.4 1.0
CG B:GLU416 4.5 9.3 1.0
O B:HOH8904 4.7 20.3 1.0
O B:ASN102 4.7 18.3 1.0
CA B:ASP201 4.8 14.6 1.0
CG2 B:VAL103 4.9 17.0 1.0
C B:GLN200 4.9 14.6 1.0
CA B:GLN200 4.9 12.9 1.0

Magnesium binding site 5 out of 12 in 1px3

Go back to Magnesium Binding Sites List in 1px3
Magnesium binding site 5 out of 12 in the E. Coli (Lacz) Beta-Galactosidase (G794A)


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 (G794A) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg3002

b:15.7
occ:1.00
 O B:ASP15 2.2 17.0 1.0
OE1 B:GLN163 2.3 16.8 1.0
OD2 B:ASP193 2.3 13.3 1.0
O B:ASN18 2.4 15.8 1.0
O B:VAL21 2.4 15.6 1.0
OD1 B:ASP193 3.0 17.4 1.0
CG B:ASP193 3.0 18.1 1.0
CD B:GLN163 3.2 13.6 1.0
C B:ASN18 3.3 16.7 1.0
C B:ASP15 3.4 15.5 1.0
NE2 B:GLN163 3.5 14.7 1.0
C B:VAL21 3.6 14.6 1.0
N B:ASN18 3.7 19.2 1.0
OH B:TYR161 3.9 17.5 1.0
CA B:ASN18 4.0 16.7 1.0
CA B:TRP16 4.0 15.8 1.0
N B:TRP16 4.2 13.8 1.0
N B:PRO19 4.2 19.1 1.0
C B:TRP16 4.3 17.6 1.0
CB B:ASN18 4.3 12.9 1.0
N B:VAL21 4.3 18.5 1.0
CA B:VAL21 4.3 14.0 1.0
CA B:PRO19 4.3 29.6 1.0
CE2 B:TYR161 4.3 14.9 1.0
CB B:VAL21 4.3 15.9 1.0
N B:GLU17 4.4 18.3 1.0
CB B:ASP193 4.5 12.1 1.0
CG B:GLN163 4.5 11.1 1.0
N B:THR22 4.5 10.7 1.0
CA B:ASP15 4.6 22.6 1.0
CA B:THR22 4.6 13.1 1.0
CZ B:TYR161 4.6 16.6 1.0
O B:TRP16 4.8 15.4 1.0
C B:PRO19 4.8 24.2 1.0
CG1 B:VAL21 4.9 19.5 1.0
C B:GLU17 4.9 18.9 1.0
CB B:ASP15 5.0 20.6 1.0

Magnesium binding site 6 out of 12 in 1px3

Go back to Magnesium Binding Sites List in 1px3
Magnesium binding site 6 out of 12 in the E. Coli (Lacz) Beta-Galactosidase (G794A)


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 (G794A) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg3001

b:15.0
occ:1.00
 O C:HOH8782 2.0 13.1 1.0
O C:HOH8705 2.1 15.4 1.0
OE2 C:GLU416 2.1 13.8 1.0
OE1 C:GLU461 2.1 14.1 1.0
O C:HOH8641 2.2 12.4 1.0
ND1 C:HIS418 2.3 16.4 1.0
CD C:GLU461 3.1 19.1 1.0
CE1 C:HIS418 3.2 15.7 1.0
CD C:GLU416 3.2 18.1 1.0
CG C:HIS418 3.4 12.1 1.0
OE1 C:GLU416 3.6 14.2 1.0
CB C:HIS418 3.6 9.1 1.0
OE2 C:GLU461 3.9 18.0 1.0
N C:ASP201 4.1 14.1 1.0
CB C:GLU461 4.1 9.2 1.0
OD1 C:ASN102 4.1 16.6 1.0
CB C:ASP201 4.2 12.3 1.0
CG C:GLU461 4.2 11.2 1.0
O C:ASP199 4.3 12.0 1.0
ND2 C:ASN460 4.3 11.3 1.0
O C:HOH8628 4.3 20.5 1.0
NE2 C:HIS418 4.3 14.1 1.0
CG C:GLU416 4.5 8.6 1.0
CD2 C:HIS418 4.5 13.8 1.0
O C:HOH8918 4.6 26.2 1.0
O C:ASN102 4.7 17.4 1.0
CA C:ASP201 4.7 13.4 1.0
C C:GLN200 4.8 21.5 1.0
CA C:GLN200 4.9 14.2 1.0
CG2 C:VAL103 4.9 17.9 1.0

Magnesium binding site 7 out of 12 in 1px3

Go back to Magnesium Binding Sites List in 1px3
Magnesium binding site 7 out of 12 in the E. Coli (Lacz) Beta-Galactosidase (G794A)


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 (G794A) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg3002

b:14.0
occ:1.00
 O C:VAL21 2.2 12.5 1.0
O C:ASP15 2.2 13.5 1.0
OE1 C:GLN163 2.4 13.5 1.0
O C:ASN18 2.4 14.5 1.0
OD2 C:ASP193 2.5 17.9 1.0
OD1 C:ASP193 3.2 20.0 1.0
CG C:ASP193 3.2 22.3 1.0
CD C:GLN163 3.3 14.2 1.0
C C:ASN18 3.3 16.4 1.0
C C:VAL21 3.3 13.9 1.0
C C:ASP15 3.4 14.3 1.0
NE2 C:GLN163 3.6 11.6 1.0
N C:ASN18 3.7 21.9 1.0
CA C:ASN18 4.0 17.1 1.0
OH C:TYR161 4.0 14.6 1.0
CA C:VAL21 4.1 12.4 1.0
CA C:TRP16 4.1 12.2 1.0
N C:PRO19 4.2 16.3 1.0
N C:TRP16 4.2 12.7 1.0
N C:VAL21 4.2 11.9 1.0
CB C:VAL21 4.2 15.5 1.0
CB C:ASN18 4.3 18.4 1.0
N C:THR22 4.3 11.4 1.0
C C:TRP16 4.3 12.4 1.0
CE2 C:TYR161 4.4 12.4 1.0
CA C:PRO19 4.4 16.5 1.0
N C:GLU17 4.5 18.4 1.0
CG C:GLN163 4.5 11.4 1.0
CA C:THR22 4.6 11.5 1.0
CA C:ASP15 4.6 16.2 1.0
CB C:ASP193 4.6 12.1 1.0
CZ C:TYR161 4.7 14.8 1.0
CG1 C:VAL21 4.7 17.9 1.0
O C:TRP16 4.8 16.8 1.0
C C:PRO19 4.9 19.1 1.0
C C:GLU17 4.9 24.6 1.0
CB C:ASP15 5.0 18.4 1.0

Magnesium binding site 8 out of 12 in 1px3

Go back to Magnesium Binding Sites List in 1px3
Magnesium binding site 8 out of 12 in the E. Coli (Lacz) Beta-Galactosidase (G794A)


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 (G794A) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg3004

b:52.9
occ:1.00
 O C:HOH9432 2.0 20.0 0.5
O C:HOH9434 2.4 37.7 1.0
CG C:GLN49 3.9 44.3 1.0
O C:HOH9276 4.3 19.6 1.0
OE2 C:GLU41 4.3 16.9 1.0
O C:HOH9466 4.5 47.5 1.0
CD C:GLN49 4.6 86.9 1.0
NE2 C:GLN49 4.7 55.9 1.0
O C:HOH9360 4.7 19.8 1.0

Magnesium binding site 9 out of 12 in 1px3

Go back to Magnesium Binding Sites List in 1px3
Magnesium binding site 9 out of 12 in the E. Coli (Lacz) Beta-Galactosidase (G794A)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 9 of E. Coli (Lacz) Beta-Galactosidase (G794A) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg3006

b:31.7
occ:1.00
 O C:HOH9459 1.8 36.3 1.0
O C:HOH9436 2.1 34.0 1.0
O C:HOH9411 2.1 32.1 1.0
O C:HOH9454 4.0 38.0 1.0
CD C:ARG178 4.2 51.9 1.0
O C:HOH9364 4.2 28.0 1.0
O C:ALA179 4.2 24.8 1.0
O C:GLU181 4.3 18.4 1.0
CG C:ARG178 4.6 32.9 1.0
N C:GLU181 4.6 16.7 1.0

Magnesium binding site 10 out of 12 in 1px3

Go back to Magnesium Binding Sites List in 1px3
Magnesium binding site 10 out of 12 in the E. Coli (Lacz) Beta-Galactosidase (G794A)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 10 of E. Coli (Lacz) Beta-Galactosidase (G794A) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg3001

b:14.7
occ:1.00
 O D:HOH8822 1.9 13.1 1.0
OE1 D:GLU461 2.0 15.3 1.0
O D:HOH8898 2.1 13.7 1.0
O D:HOH8759 2.1 12.4 1.0
ND1 D:HIS418 2.2 16.2 1.0
OE2 D:GLU416 2.2 15.4 1.0
CE1 D:HIS418 3.0 18.3 1.0
CD D:GLU461 3.1 24.2 1.0
CD D:GLU416 3.3 13.0 1.0
CG D:HIS418 3.3 12.0 1.0
OE1 D:GLU416 3.7 14.1 1.0
CB D:HIS418 3.8 11.3 1.0
OE2 D:GLU461 3.9 20.1 1.0
CB D:ASP201 4.1 14.8 1.0
CB D:GLU461 4.1 9.3 1.0
CG D:GLU461 4.1 11.9 1.0
O D:HOH8746 4.2 19.8 1.0
N D:ASP201 4.2 14.7 1.0
OD1 D:ASN102 4.2 21.1 1.0
NE2 D:HIS418 4.3 16.2 1.0
ND2 D:ASN460 4.3 12.1 1.0
O D:ASP199 4.3 13.5 1.0
CD2 D:HIS418 4.4 15.2 1.0
CG D:GLU416 4.5 9.0 1.0
O D:HOH9033 4.5 19.5 1.0
O D:ASN102 4.7 18.3 1.0
CA D:ASP201 4.7 14.8 1.0
O D:HOH9020 4.9 35.3 1.0
CA D:GLN200 4.9 13.2 1.0
C D:GLN200 4.9 14.5 1.0

Reference:

D.H.Juers, S.Hakda, B.W.Matthews, R.E.Huber. Structural Basis For the Altered Activity of GLY794 Variants of Escherichia Coli Beta-Galactosidase Biochemistry V. 42 13505 2003.
ISSN: ISSN 0006-2960
PubMed: 14621996
DOI: 10.1021/BI035506J
Page generated: Tue Aug 13 10:57:09 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