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Zinc in PDB 1ajb: Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity

Enzymatic activity of Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity

All present enzymatic activity of Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity:
3.1.3.1;

Protein crystallography data

The structure of Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity, PDB code: 1ajb was solved by C.G.Dealwis, L.Chen, C.Abad-Zapatero, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.50
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 195.020, 166.930, 76.440, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / n/a

Other elements in 1ajb:

The structure of Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity (pdb code 1ajb). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity, PDB code: 1ajb:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1ajb

Go back to Zinc Binding Sites List in 1ajb
Zinc binding site 1 out of 4 in the Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn450

b:10.1
occ:1.00
OD1 A:ASP327 2.3 5.3 1.0
NE2 A:HIS412 2.3 2.0 1.0
NE2 A:HIS331 2.5 3.3 1.0
OD2 A:ASP327 2.5 7.2 1.0
CG A:ASP327 2.7 6.2 1.0
CD2 A:HIS331 3.0 4.4 1.0
CD2 A:HIS412 3.1 8.3 1.0
CE1 A:HIS412 3.4 2.9 1.0
CE1 A:HIS331 3.6 6.0 1.0
OG A:SER102 4.1 3.3 1.0
NE2 A:HIS372 4.1 2.0 1.0
CB A:ASP327 4.3 7.4 1.0
NE2 A:HIS370 4.3 9.5 1.0
CG A:HIS331 4.3 9.0 1.0
O A:HOH543 4.3 0.0 0.0
CG A:HIS412 4.3 6.7 1.0
ZN A:ZN451 4.4 18.2 1.0
ND1 A:HIS412 4.4 8.6 1.0
CE1 A:HIS370 4.5 9.3 1.0
ND1 A:HIS331 4.5 11.7 1.0
OD1 A:ASP51 4.6 7.4 1.0
O4 A:SO4457 4.6 23.2 1.0
O A:ASP327 4.6 6.5 1.0
O A:HOH544 4.8 30.5 1.0
O A:HOH547 4.9 0.0 0.0
CE1 A:HIS372 4.9 2.2 1.0
CD2 A:HIS372 4.9 2.0 1.0

Zinc binding site 2 out of 4 in 1ajb

Go back to Zinc Binding Sites List in 1ajb
Zinc binding site 2 out of 4 in the Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn451

b:18.2
occ:1.00
OD1 A:ASP51 1.9 7.4 1.0
OG A:SER102 1.9 3.3 1.0
OD2 A:ASP369 2.2 5.8 1.0
NE2 A:HIS370 2.4 9.5 1.0
CG A:ASP51 2.8 8.8 1.0
CG A:ASP369 3.0 7.3 1.0
OD2 A:ASP51 3.0 13.1 1.0
CD2 A:HIS370 3.1 9.9 1.0
OD1 A:ASP369 3.1 7.3 1.0
CB A:SER102 3.2 2.0 1.0
CE1 A:HIS370 3.4 9.3 1.0
CA A:SER102 3.5 3.2 1.0
OD1 A:ASP327 3.9 5.3 1.0
O A:HOH478 4.0 9.8 1.0
N A:SER102 4.2 2.0 1.0
CB A:ASP51 4.2 4.2 1.0
CG A:HIS370 4.2 7.2 1.0
O A:HOH458 4.2 0.0 0.0
CG A:ASP327 4.3 6.2 1.0
ND1 A:HIS370 4.3 9.7 1.0
CB A:ASP369 4.3 6.5 1.0
ZN A:ZN450 4.4 10.1 1.0
N A:GLY52 4.4 2.6 1.0
CE1 A:HIS412 4.4 2.9 1.0
CA A:ASP51 4.5 4.8 1.0
NE2 A:HIS412 4.6 2.0 1.0
MG A:MG452 4.6 26.2 1.0
OD2 A:ASP327 4.7 7.2 1.0
C A:ASP51 4.7 3.0 1.0
C A:SER102 4.8 3.0 1.0
C A:ASP101 4.8 4.1 1.0
CB A:ASP327 4.9 7.4 1.0
O A:SER102 5.0 4.2 1.0
OG A:SER105 5.0 2.0 1.0

Zinc binding site 3 out of 4 in 1ajb

Go back to Zinc Binding Sites List in 1ajb
Zinc binding site 3 out of 4 in the Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn950

b:15.9
occ:1.00
OD1 B:ASP327 2.4 15.0 1.0
OD2 B:ASP327 2.4 12.3 1.0
NE2 B:HIS331 2.4 7.3 1.0
NE2 B:HIS412 2.6 19.1 1.0
CG B:ASP327 2.7 14.1 1.0
CD2 B:HIS331 3.2 7.9 1.0
CD2 B:HIS412 3.3 21.9 1.0
CE1 B:HIS331 3.5 11.6 1.0
CE1 B:HIS412 3.7 19.8 1.0
OG B:SER102 3.9 4.7 1.0
CB B:ASP327 4.2 16.2 1.0
O B:HOH972 4.3 2.0 1.0
NE2 B:HIS372 4.3 8.7 1.0
O2 B:SO4957 4.3 28.1 1.0
CG B:HIS331 4.4 11.0 1.0
CE1 B:HIS370 4.4 5.2 1.0
CG B:HIS412 4.5 20.7 1.0
ND1 B:HIS331 4.5 14.9 1.0
NE2 B:HIS370 4.5 4.3 1.0
ZN B:ZN951 4.5 16.1 1.0
ND1 B:HIS412 4.6 23.8 1.0
O B:ASP327 4.7 17.1 1.0
OD1 B:ASP51 4.7 8.9 1.0
CD2 B:HIS372 4.8 2.0 1.0
O B:HOH958 4.9 10.9 1.0

Zinc binding site 4 out of 4 in 1ajb

Go back to Zinc Binding Sites List in 1ajb
Zinc binding site 4 out of 4 in the Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Three-Dimensional Structure of the D153G Mutant of E. Coli Alkaline Phosphatase: A Mutant with Weaker Magnesium Binding and Increased Catalytic Activity within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn951

b:16.1
occ:1.00
OD1 B:ASP51 1.9 8.9 1.0
OG B:SER102 2.0 4.7 1.0
OD2 B:ASP369 2.1 12.0 1.0
NE2 B:HIS370 2.2 4.3 1.0
CB B:SER102 2.8 6.0 1.0
CG B:ASP51 2.8 10.7 1.0
CG B:ASP369 2.9 9.6 1.0
OD1 B:ASP369 3.0 8.7 1.0
OD2 B:ASP51 3.1 14.4 1.0
CD2 B:HIS370 3.1 5.4 1.0
CE1 B:HIS370 3.2 5.2 1.0
CA B:SER102 3.5 9.2 1.0
O B:HOH958 3.8 10.9 1.0
OD1 B:ASP327 4.0 15.0 1.0
CB B:ASP51 4.2 10.1 1.0
N B:SER102 4.2 9.9 1.0
ND1 B:HIS370 4.2 9.8 1.0
CG B:HIS370 4.2 8.0 1.0
CB B:ASP369 4.3 7.5 1.0
CG B:ASP327 4.3 14.1 1.0
N B:GLY52 4.5 2.9 1.0
ZN B:ZN950 4.5 15.9 1.0
CA B:ASP51 4.6 6.2 1.0
C B:ASP51 4.7 5.6 1.0
C B:SER102 4.8 7.8 1.0
OD2 B:ASP327 4.8 12.3 1.0
CE1 B:HIS412 4.8 19.8 1.0
CB B:ASP327 4.9 16.2 1.0
C B:ASP101 4.9 7.1 1.0
OG1 B:THR155 4.9 13.2 1.0
OG B:SER105 4.9 2.0 1.0
O B:SER102 5.0 10.7 1.0
NE2 B:HIS412 5.0 19.1 1.0

Reference:

C.G.Dealwis, L.Chen, C.Brennan, W.Mandecki, C.Abad-Zapatero. 3-D Structure of the D153G Mutant of Escherichia Coli Alkaline Phosphatase: An Enzyme with Weaker Magnesium Binding and Increased Catalytic Activity. Protein Eng. V. 8 865 1995.
ISSN: ISSN 0269-2139
PubMed: 8746724
DOI: 10.1093/PROTEIN/8.9.865
Page generated: Wed Dec 16 02:44:42 2020

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