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Zinc in PDB 1ajc: 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: 1ajc 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 1ajc:

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 1ajc). 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: 1ajc:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1ajc

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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:49.9
occ:0.94
 NE2 A:HIS412 2.0 10.5 1.0
OD2 A:ASP327 2.1 13.6 1.0
OD1 A:ASP327 2.2 12.9 1.0
NE2 A:HIS331 2.2 13.7 1.0
CG A:ASP327 2.5 9.7 1.0
CE1 A:HIS412 2.8 14.9 1.0
CD2 A:HIS412 3.0 13.8 1.0
CE1 A:HIS370 3.2 12.8 1.0
CE1 A:HIS331 3.2 17.7 1.0
NE2 A:HIS370 3.2 10.5 1.0
CD2 A:HIS331 3.2 14.3 1.0
CE1 A:HIS372 3.2 22.8 1.0
ZN A:ZN451 3.7 52.3 1.0
NE2 A:HIS372 3.8 24.3 1.0
ND1 A:HIS412 3.8 12.2 1.0
CG A:HIS412 3.9 13.2 1.0
CB A:ASP327 4.0 13.8 1.0
OG A:SER102 4.0 21.9 1.0
ND1 A:HIS372 4.3 25.4 1.0
ND1 A:HIS331 4.4 15.4 1.0
CG A:HIS331 4.4 15.9 1.0
ND1 A:HIS370 4.5 14.2 1.0
CD2 A:HIS370 4.6 12.5 1.0
O A:ASP327 4.8 8.6 1.0
CA A:ASP327 4.8 7.6 1.0
C A:ASP327 4.9 8.5 1.0

Zinc binding site 2 out of 4 in 1ajc

Go back to Zinc Binding Sites List in 1ajc
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:52.3
occ:1.00
 OD2 A:ASP369 2.0 12.1 1.0
OG A:SER102 2.1 21.9 1.0
NE2 A:HIS370 2.3 10.5 1.0
OD2 A:ASP327 2.8 13.6 1.0
CE1 A:HIS370 2.8 12.8 1.0
CG A:ASP369 2.9 14.5 1.0
OD2 A:ASP51 3.0 24.4 1.0
CD2 A:HIS370 3.1 12.5 1.0
OD1 A:ASP369 3.2 13.0 1.0
CG A:ASP51 3.3 22.4 1.0
CB A:SER102 3.4 19.0 1.0
CG A:ASP327 3.7 9.7 1.0
ZN A:ZN450 3.7 49.9 0.9
ND1 A:HIS370 3.7 14.2 1.0
OD1 A:ASP51 3.8 24.4 1.0
CG A:HIS370 3.9 9.9 1.0
CB A:ASP51 3.9 10.0 1.0
CA A:SER102 4.0 14.2 1.0
N A:GLY52 4.2 8.4 1.0
C A:ASP51 4.3 13.1 1.0
CA A:ASP51 4.3 10.5 1.0
CB A:ASP369 4.3 8.6 1.0
OD1 A:ASP327 4.4 12.9 1.0
CB A:ASP327 4.4 13.8 1.0
N A:SER102 4.4 15.2 1.0
CE1 A:HIS412 4.6 14.9 1.0
MG A:MG452 4.8 14.3 1.0
NE2 A:HIS412 4.8 10.5 1.0
CA A:GLY52 4.8 9.5 1.0
O A:ASP51 4.9 10.7 1.0
N A:HIS370 5.0 11.7 1.0

Zinc binding site 3 out of 4 in 1ajc

Go back to Zinc Binding Sites List in 1ajc
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:50.8
occ:0.94
 NE2 B:HIS412 2.1 15.7 1.0
OD1 B:ASP327 2.2 21.8 1.0
NE2 B:HIS331 2.2 10.0 1.0
OD2 B:ASP327 2.2 25.3 1.0
CG B:ASP327 2.5 15.6 1.0
CE1 B:HIS412 2.8 15.5 1.0
CD2 B:HIS331 3.0 16.9 1.0
CD2 B:HIS412 3.2 15.9 1.0
CE1 B:HIS331 3.3 14.6 1.0
CE1 B:HIS372 3.6 24.0 1.0
CE1 B:HIS370 3.8 11.8 1.0
NE2 B:HIS370 3.9 14.4 1.0
OG B:SER102 3.9 22.4 1.0
ZN B:ZN951 3.9 47.9 1.0
ND1 B:HIS412 4.0 12.1 1.0
CB B:ASP327 4.0 18.3 1.0
CG B:HIS412 4.2 15.6 1.0
CG B:HIS331 4.2 17.3 1.0
ND1 B:HIS331 4.3 19.6 1.0
NE2 B:HIS372 4.4 20.2 1.0
ND1 B:HIS372 4.6 24.2 1.0
O B:ASP327 4.8 17.6 1.0
C B:ASP327 4.9 15.3 1.0
CA B:ASP327 4.9 13.3 1.0

Zinc binding site 4 out of 4 in 1ajc

Go back to Zinc Binding Sites List in 1ajc
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:47.9
occ:0.99
 OD2 B:ASP369 2.0 16.4 1.0
OG B:SER102 2.1 22.4 1.0
NE2 B:HIS370 2.2 14.4 1.0
OD1 B:ASP51 2.8 23.1 1.0
CG B:ASP369 2.8 16.6 1.0
CD2 B:HIS370 3.0 11.7 1.0
OD1 B:ASP369 3.0 18.9 1.0
OD2 B:ASP327 3.1 25.3 1.0
CE1 B:HIS370 3.2 11.8 1.0
CB B:SER102 3.3 23.1 1.0
CG B:ASP51 3.4 22.2 1.0
CG B:ASP327 3.7 15.6 1.0
ZN B:ZN950 3.9 50.8 0.9
CA B:SER102 4.0 17.8 1.0
OD2 B:ASP51 4.0 24.3 1.0
CG B:HIS370 4.1 11.5 1.0
CB B:ASP51 4.2 13.5 1.0
CB B:ASP327 4.2 18.3 1.0
ND1 B:HIS370 4.2 10.7 1.0
CB B:ASP369 4.3 15.6 1.0
N B:GLY52 4.3 13.1 1.0
CA B:ASP51 4.4 16.8 1.0
CE1 B:HIS412 4.4 15.5 1.0
OD1 B:ASP327 4.4 21.8 1.0
N B:SER102 4.5 15.2 1.0
C B:ASP51 4.6 14.3 1.0
NE2 B:HIS412 4.7 15.7 1.0
O B:HOH956 4.7 18.0 1.0
MG B:MG952 4.9 24.5 1.0

Reference:

C.G.Dealwis, C.Brennan, K.Christianson, W.Mandecki, C.Abad-Zapatero. Crystallographic Analysis of Reversible Metal Binding Observed in A Mutant (ASP153-->Gly) of Escherichia Coli Alkaline Phosphatase. Biochemistry V. 34 13967 1995.
ISSN: ISSN 0006-2960
PubMed: 7577993
DOI: 10.1021/BI00043A001
Page generated: Sat Oct 12 22:03:55 2024

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