Atomistry » Magnesium » PDB 1eo3-1f6t » 1f4h
Atomistry »
  Magnesium »
    PDB 1eo3-1f6t »
      1f4h »

Magnesium in PDB 1f4h: E. Coli (Lacz) Beta-Galactosidase (Orthorhombic)

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

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

Protein crystallography data

The structure of E. Coli (Lacz) Beta-Galactosidase (Orthorhombic), PDB code: 1f4h was solved by D.H.Juers, R.H.Jacobson, D.Wigley, X.J.Zhang, R.E.Huber, D.E.Tronrud, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 153.400, 173.400, 204.400, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Magnesium Binding Sites:

The binding sites of Magnesium atom in the E. Coli (Lacz) Beta-Galactosidase (Orthorhombic) (pdb code 1f4h). 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 (Orthorhombic), PDB code: 1f4h:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Magnesium binding site 1 out of 8 in 1f4h

Go back to Magnesium Binding Sites List in 1f4h
Magnesium binding site 1 out of 8 in the E. Coli (Lacz) Beta-Galactosidase (Orthorhombic)


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

b:28.1
occ:1.00
 OE2 A:GLU461 2.3 47.9 1.0
O A:HOH4008 2.4 27.9 1.0
ND1 A:HIS418 2.5 29.6 1.0
OE1 A:GLU416 2.6 5.9 1.0
ND2 A:ASN102 3.1 31.8 1.0
CE1 A:HIS418 3.4 26.0 1.0
CD A:GLU461 3.4 42.9 1.0
CG A:HIS418 3.5 25.2 1.0
CD A:GLU416 3.7 24.1 1.0
CB A:HIS418 3.8 17.1 1.0
CB A:ASP201 3.9 41.7 1.0
OE1 A:GLU461 3.9 11.8 1.0
O A:ASN102 3.9 37.1 1.0
N A:ASP201 3.9 18.4 1.0
OE2 A:GLU416 4.2 14.8 1.0
O A:ASP199 4.3 5.8 1.0
CA A:ASP201 4.3 30.1 1.0
C A:ASN102 4.4 33.8 1.0
O A:HOH4001 4.4 33.4 1.0
CG A:ASN102 4.5 71.2 1.0
CG A:GLU461 4.6 16.9 1.0
NE2 A:HIS418 4.6 26.3 1.0
CD2 A:HIS418 4.7 31.2 1.0
N A:VAL103 4.7 19.2 1.0
CA A:VAL103 4.7 16.5 1.0
C A:GLN200 4.7 23.6 1.0
CG2 A:VAL103 4.8 13.5 1.0
CG A:GLU416 4.9 20.4 1.0
CA A:GLN200 4.9 18.4 1.0
CG A:ASP201 5.0 59.8 1.0

Magnesium binding site 2 out of 8 in 1f4h

Go back to Magnesium Binding Sites List in 1f4h
Magnesium binding site 2 out of 8 in the E. Coli (Lacz) Beta-Galactosidase (Orthorhombic)


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

b:31.4
occ:1.00
 O A:VAL21 2.1 29.4 1.0
NE2 A:GLN163 2.2 1.0 1.0
O A:ASN18 2.3 20.8 1.0
O A:ASP15 2.3 27.9 1.0
OD2 A:ASP193 2.3 5.0 1.0
CD A:GLN163 3.1 27.3 1.0
C A:ASN18 3.1 23.2 1.0
CG A:ASP193 3.1 25.2 1.0
OD1 A:ASP193 3.1 9.3 1.0
OE1 A:GLN163 3.3 27.3 1.0
C A:VAL21 3.3 16.2 1.0
C A:ASP15 3.5 21.8 1.0
N A:ASN18 3.7 18.2 1.0
CA A:ASN18 3.7 13.2 1.0
CB A:VAL21 3.9 18.9 1.0
CA A:VAL21 3.9 15.9 1.0
N A:VAL21 3.9 23.1 1.0
N A:PRO19 4.1 20.0 1.0
CB A:ASN18 4.1 9.8 1.0
CE2 A:TYR161 4.2 16.2 1.0
OH A:TYR161 4.2 30.9 1.0
CA A:TRP16 4.3 24.7 1.0
N A:THR22 4.3 6.6 1.0
CG1 A:VAL21 4.3 15.3 1.0
N A:TRP16 4.3 19.3 1.0
CG A:GLN163 4.4 17.7 1.0
C A:TRP16 4.5 20.2 1.0
CA A:PRO19 4.5 16.6 1.0
CA A:ASP15 4.5 28.6 1.0
CB A:ASP193 4.5 5.3 1.0
CA A:THR22 4.6 10.4 1.0
N A:GLU17 4.6 4.4 1.0
CZ A:TYR161 4.7 22.4 1.0
C A:PRO19 4.7 19.7 1.0
CB A:ASP15 4.8 37.6 1.0
CG A:ASN18 4.8 46.5 1.0
N A:GLY20 4.9 8.2 1.0
O A:TRP16 5.0 28.8 1.0
C A:GLU17 5.0 29.0 1.0

Magnesium binding site 3 out of 8 in 1f4h

Go back to Magnesium Binding Sites List in 1f4h
Magnesium binding site 3 out of 8 in the E. Coli (Lacz) Beta-Galactosidase (Orthorhombic)


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

b:20.7
occ:1.00
 O B:HOH4014 2.0 7.1 1.0
O B:HOH4156 2.2 21.6 1.0
ND1 B:HIS418 2.3 31.7 1.0
OE2 B:GLU461 2.5 44.7 1.0
CE1 B:HIS418 2.6 27.3 1.0
ND2 B:ASN102 2.8 52.8 1.0
OE1 B:GLU416 3.0 1.0 1.0
CD B:GLU461 3.2 26.2 1.0
OE1 B:GLU461 3.3 28.9 1.0
O B:HOH4568 3.3 23.6 1.0
O B:HOH4001 3.5 41.5 1.0
CG B:HIS418 3.6 33.7 1.0
O B:HOH4298 3.6 45.2 1.0
CB B:ASP201 3.8 26.4 1.0
NE2 B:HIS418 3.9 24.1 1.0
CG B:ASN102 4.0 39.8 1.0
CG2 B:VAL103 4.1 32.3 1.0
CD B:GLU416 4.1 54.2 1.0
N B:ASP201 4.3 20.0 1.0
OD1 B:ASN102 4.4 51.5 1.0
CD2 B:HIS418 4.4 29.5 1.0
CB B:HIS418 4.4 31.4 1.0
CA B:ASP201 4.6 21.9 1.0
CG B:GLU461 4.6 1.0 1.0
OE2 B:GLU416 4.6 1.0 1.0
O B:ASN102 4.7 27.4 1.0
CG B:ASP201 4.9 56.5 1.0
C B:ASN102 4.9 37.5 1.0
CB B:GLU461 5.0 18.4 1.0
O B:ASP199 5.0 24.3 1.0

Magnesium binding site 4 out of 8 in 1f4h

Go back to Magnesium Binding Sites List in 1f4h
Magnesium binding site 4 out of 8 in the E. Coli (Lacz) Beta-Galactosidase (Orthorhombic)


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

b:36.5
occ:1.00
 O B:ASN18 2.0 31.4 1.0
O B:VAL21 2.1 41.8 1.0
OD2 B:ASP193 2.2 8.5 1.0
O B:ASP15 2.4 39.0 1.0
NE2 B:GLN163 2.6 79.7 1.0
C B:ASN18 2.9 24.5 1.0
CG B:ASP193 3.0 37.1 1.0
OE1 B:GLN163 3.1 44.0 1.0
OD1 B:ASP193 3.1 42.7 1.0
CD B:GLN163 3.1 35.3 1.0
C B:VAL21 3.3 38.3 1.0
N B:PRO19 3.6 29.0 1.0
C B:ASP15 3.6 32.8 1.0
N B:ASN18 3.7 16.8 1.0
CA B:PRO19 3.8 25.3 1.0
CA B:ASN18 3.8 12.1 1.0
CA B:VAL21 4.1 20.4 1.0
N B:VAL21 4.1 25.4 1.0
CB B:VAL21 4.2 15.7 1.0
CA B:TRP16 4.3 22.2 1.0
N B:THR22 4.3 27.5 1.0
CB B:ASP193 4.4 11.9 1.0
C B:PRO19 4.4 32.5 1.0
CG1 B:VAL21 4.4 16.4 1.0
N B:TRP16 4.4 14.9 1.0
C B:TRP16 4.4 31.5 1.0
CE2 B:TYR161 4.5 22.3 1.0
CB B:ASN18 4.5 35.1 1.0
CG B:GLN163 4.5 29.9 1.0
CA B:THR22 4.5 24.4 1.0
N B:GLY20 4.5 31.8 1.0
N B:GLU17 4.6 21.2 1.0
CA B:ASP15 4.7 40.0 1.0
OH B:TYR161 4.7 18.9 1.0
C B:GLU17 4.9 33.3 1.0
CG B:ASN18 4.9 48.2 1.0
O B:TRP16 4.9 33.7 1.0
CB B:ASP15 5.0 43.0 1.0
N B:ASP193 5.0 11.4 1.0

Magnesium binding site 5 out of 8 in 1f4h

Go back to Magnesium Binding Sites List in 1f4h
Magnesium binding site 5 out of 8 in the E. Coli (Lacz) Beta-Galactosidase (Orthorhombic)


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

b:15.7
occ:1.00
 O C:HOH4156 2.2 10.2 1.0
ND1 C:HIS418 2.5 32.2 1.0
O C:HOH4014 2.5 6.8 1.0
OE2 C:GLU461 2.6 68.2 1.0
CE1 C:HIS418 2.9 30.5 1.0
CD C:GLU461 2.9 45.2 1.0
OE1 C:GLU461 3.2 16.9 1.0
ND2 C:ASN102 3.3 28.0 1.0
OE1 C:GLU416 3.4 8.0 1.0
O C:HOH4001 3.5 38.0 1.0
O C:HOH4568 3.6 20.2 1.0
O C:HOH7520 3.7 34.1 1.0
CG C:GLU461 3.7 7.5 1.0
CB C:ASP201 3.7 26.9 1.0
CG C:HIS418 3.8 28.8 1.0
NE2 C:HIS418 4.2 30.2 1.0
CD C:GLU416 4.5 29.4 1.0
N C:ASP201 4.5 16.8 1.0
CG C:ASN102 4.5 49.4 1.0
CB C:HIS418 4.5 24.4 1.0
CD2 C:HIS418 4.7 29.8 1.0
CA C:ASP201 4.7 21.8 1.0
CG C:ASP201 4.7 38.8 1.0
ND2 C:ASN460 4.7 17.7 1.0
CG2 C:VAL103 4.8 21.9 1.0
OE2 C:GLU416 4.8 13.7 1.0
OD2 C:ASP201 4.9 63.8 1.0
OD1 C:ASN102 4.9 39.4 1.0
O C:ASN102 4.9 50.1 1.0

Magnesium binding site 6 out of 8 in 1f4h

Go back to Magnesium Binding Sites List in 1f4h
Magnesium binding site 6 out of 8 in the E. Coli (Lacz) Beta-Galactosidase (Orthorhombic)


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

b:31.8
occ:1.00
 O C:ASN18 2.2 28.1 1.0
OD2 C:ASP193 2.3 11.9 1.0
NE2 C:GLN163 2.4 38.7 1.0
O C:VAL21 2.5 43.7 1.0
O C:ASP15 2.6 45.3 1.0
CD C:GLN163 2.8 19.6 1.0
OE1 C:GLN163 2.9 35.9 1.0
CG C:ASP193 3.2 29.3 1.0
C C:ASN18 3.3 27.9 1.0
C C:VAL21 3.3 34.9 1.0
OD1 C:ASP193 3.4 46.9 1.0
C C:ASP15 3.7 39.0 1.0
N C:ASN18 3.9 22.9 1.0
CG C:GLN163 4.0 5.0 1.0
CA C:ASN18 4.1 19.6 1.0
CA C:VAL21 4.1 13.3 1.0
N C:THR22 4.1 35.5 1.0
OH C:TYR161 4.1 34.2 1.0
N C:VAL21 4.2 21.5 1.0
CE2 C:TYR161 4.2 12.0 1.0
N C:PRO19 4.2 30.4 1.0
CA C:PRO19 4.3 30.5 1.0
CA C:THR22 4.3 25.9 1.0
CA C:TRP16 4.3 25.2 1.0
CB C:VAL21 4.4 13.9 1.0
N C:TRP16 4.5 33.3 1.0
CB C:ASN18 4.5 17.8 1.0
CB C:ASP193 4.6 18.6 1.0
C C:TRP16 4.6 35.8 1.0
CZ C:TYR161 4.6 15.0 1.0
N C:GLU17 4.7 25.7 1.0
CA C:ASP15 4.8 30.9 1.0
C C:PRO19 4.8 46.0 1.0
CG1 C:VAL21 4.9 13.1 1.0
N C:GLY20 5.0 42.3 1.0

Magnesium binding site 7 out of 8 in 1f4h

Go back to Magnesium Binding Sites List in 1f4h
Magnesium binding site 7 out of 8 in the E. Coli (Lacz) Beta-Galactosidase (Orthorhombic)


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

b:40.2
occ:1.00
 OE2 D:GLU461 1.6 64.4 1.0
O D:HOH4014 2.0 28.9 1.0
O D:HOH4156 2.0 35.5 1.0
OE1 D:GLU416 2.8 9.2 1.0
ND1 D:HIS418 2.8 26.8 1.0
CD D:GLU461 2.9 46.4 1.0
CE1 D:HIS418 3.3 23.6 1.0
ND2 D:ASN102 3.6 34.2 1.0
OE1 D:GLU461 3.6 18.4 1.0
CD D:GLU416 3.7 20.4 1.0
CG D:GLU461 3.8 25.6 1.0
OE2 D:GLU416 3.9 1.0 1.0
O D:HOH4298 3.9 26.8 1.0
CB D:ASP201 3.9 35.2 1.0
CG D:HIS418 4.0 24.5 1.0
N D:ASP201 4.1 24.9 1.0
ND2 D:ASN460 4.3 37.2 1.0
O D:HOH4568 4.3 48.9 1.0
O D:ASN102 4.6 58.9 1.0
CA D:ASP201 4.6 28.9 1.0
CB D:HIS418 4.6 17.8 1.0
NE2 D:HIS418 4.6 22.6 1.0
O D:ASP199 4.8 17.5 1.0
CG D:ASN102 4.9 40.2 1.0
CB D:GLU461 4.9 11.8 1.0
CD2 D:HIS418 5.0 25.1 1.0

Magnesium binding site 8 out of 8 in 1f4h

Go back to Magnesium Binding Sites List in 1f4h
Magnesium binding site 8 out of 8 in the E. Coli (Lacz) Beta-Galactosidase (Orthorhombic)


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

b:25.4
occ:1.00
 OD2 D:ASP193 2.0 2.7 1.0
O D:ASN18 2.1 25.1 1.0
NE2 D:GLN163 2.2 1.0 1.0
O D:VAL21 2.5 6.0 1.0
O D:ASP15 2.6 28.2 1.0
CG D:ASP193 2.8 18.6 1.0
C D:ASN18 2.8 25.6 1.0
OD1 D:ASP193 2.9 26.0 1.0
CD D:GLN163 3.0 23.9 1.0
OE1 D:GLN163 3.0 20.5 1.0
N D:PRO19 3.6 14.5 1.0
N D:ASN18 3.6 21.9 1.0
C D:VAL21 3.7 10.5 1.0
CA D:ASN18 3.7 18.2 1.0
C D:ASP15 3.8 23.4 1.0
CA D:PRO19 3.9 5.5 1.0
CB D:ASP193 4.1 6.8 1.0
OH D:TYR161 4.2 17.3 1.0
CA D:TRP16 4.2 24.1 1.0
C D:TRP16 4.4 16.6 1.0
N D:GLU17 4.4 12.5 1.0
N D:TRP16 4.4 23.6 1.0
O D:HOH4147 4.4 26.7 1.0
CG D:GLN163 4.4 16.1 1.0
CB D:ASN18 4.5 3.4 1.0
N D:THR22 4.5 1.5 1.0
CA D:THR22 4.5 3.8 1.0
C D:PRO19 4.6 21.4 1.0
CE2 D:TYR161 4.7 14.8 1.0
CA D:VAL21 4.8 9.1 1.0
N D:GLY20 4.8 21.9 1.0
N D:VAL21 4.8 12.7 1.0
C D:GLU17 4.8 27.8 1.0
CB D:VAL21 4.8 13.0 1.0
N D:ASP193 4.9 17.6 1.0
CD D:PRO19 4.9 11.0 1.0
CG D:ASN18 4.9 39.8 1.0
CG2 D:THR22 4.9 20.0 1.0
CZ D:TYR161 4.9 1.0 1.0
CA D:ASP15 5.0 15.6 1.0
CA D:ASP193 5.0 8.3 1.0
N D:GLY194 5.0 6.2 1.0

Reference:

D.H.Juers, R.H.Jacobson, D.Wigley, X.J.Zhang, R.E.Huber, D.E.Tronrud, B.W.Matthews. High Resolution Refinement of Beta-Galactosidase in A New Crystal Form Reveals Multiple Metal-Binding Sites and Provides A Structural Basis For Alpha-Complementation. Protein Sci. V. 9 1685 2000.
ISSN: ISSN 0961-8368
PubMed: 11045615
Page generated: Sat Aug 9 20:52:03 2025

Last articles

Mg in 4ZKD
Mg in 4ZK5
Mg in 4ZJJ
Mg in 4ZJI
Mg in 4ZK4
Mg in 4ZIR
Mg in 4ZIY
Mg in 4ZIB
Mg in 4ZI7
Mg in 4ZIL
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy