Atomistry » Zinc » PDB 1adf-1axg » 1ajc
Atomistry »
  Zinc »
    PDB 1adf-1axg »
      1ajc »

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

Go back to Zinc Binding Sites List in 1ajc
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

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