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Zinc in PDB 1alh: Kinetics and Crystal Structure of A Mutant E. Coli Alkaline Phosphatase (Asp-369-->Asn): A Mechanism Involving One Zinc Per Active Site

Enzymatic activity of Kinetics and Crystal Structure of A Mutant E. Coli Alkaline Phosphatase (Asp-369-->Asn): A Mechanism Involving One Zinc Per Active Site

All present enzymatic activity of Kinetics and Crystal Structure of A Mutant E. Coli Alkaline Phosphatase (Asp-369-->Asn): A Mechanism Involving One Zinc Per Active Site:
3.1.3.1;

Protein crystallography data

The structure of Kinetics and Crystal Structure of A Mutant E. Coli Alkaline Phosphatase (Asp-369-->Asn): A Mechanism Involving One Zinc Per Active Site, PDB code: 1alh was solved by T.T.Tibbitts, X.Xu, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.50
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 194.392, 167.251, 76.320, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Kinetics and Crystal Structure of A Mutant E. Coli Alkaline Phosphatase (Asp-369-->Asn): A Mechanism Involving One Zinc Per Active Site (pdb code 1alh). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Kinetics and Crystal Structure of A Mutant E. Coli Alkaline Phosphatase (Asp-369-->Asn): A Mechanism Involving One Zinc Per Active Site, PDB code: 1alh:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1alh

Go back to Zinc Binding Sites List in 1alh
Zinc binding site 1 out of 2 in the Kinetics and Crystal Structure of A Mutant E. Coli Alkaline Phosphatase (Asp-369-->Asn): A Mechanism Involving One Zinc Per Active Site


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Kinetics and Crystal Structure of A Mutant E. Coli Alkaline Phosphatase (Asp-369-->Asn): A Mechanism Involving One Zinc Per Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn450

b:27.7
occ:1.00
 O1 A:PO4453 1.9 74.8 1.0
NE2 A:HIS331 2.2 34.3 1.0
OD2 A:ASP327 2.4 41.6 1.0
NE2 A:HIS412 2.4 39.0 1.0
OD1 A:ASP327 2.5 17.0 1.0
CG A:ASP327 2.8 35.7 1.0
CD2 A:HIS412 3.0 37.2 1.0
CE1 A:HIS331 3.0 35.0 1.0
P A:PO4453 3.0 74.1 1.0
O3 A:PO4453 3.2 74.6 1.0
CD2 A:HIS331 3.3 33.6 1.0
HE2 A:HIS372 3.5 0.0 1.0
CE1 A:HIS412 3.6 39.0 1.0
HG A:SER102 3.6 0.0 1.0
CE1 A:HIS370 3.8 21.2 1.0
O2 A:PO4453 3.8 67.4 1.0
OG A:SER102 3.8 23.7 1.0
NE2 A:HIS370 3.8 23.1 1.0
NE2 A:HIS372 3.9 24.3 1.0
ND1 A:HIS331 4.2 36.8 1.0
O4 A:PO4453 4.2 76.9 1.0
CG A:HIS412 4.2 31.5 1.0
CB A:ASP327 4.3 37.9 1.0
CG A:HIS331 4.3 35.6 1.0
ND1 A:HIS412 4.5 37.1 1.0
OD1 A:ASP51 4.5 43.8 1.0
CE1 A:HIS372 4.5 28.1 1.0
H A:SER102 4.6 0.0 1.0
CD2 A:HIS372 4.7 20.5 1.0
HD21 A:ASN369 4.8 0.0 1.0
O A:ASP327 4.9 39.1 1.0
ND1 A:HIS370 5.0 17.7 1.0

Zinc binding site 2 out of 2 in 1alh

Go back to Zinc Binding Sites List in 1alh
Zinc binding site 2 out of 2 in the Kinetics and Crystal Structure of A Mutant E. Coli Alkaline Phosphatase (Asp-369-->Asn): A Mechanism Involving One Zinc Per Active Site


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Kinetics and Crystal Structure of A Mutant E. Coli Alkaline Phosphatase (Asp-369-->Asn): A Mechanism Involving One Zinc Per Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn450

b:37.7
occ:1.00
 O1 B:PO4453 2.0 70.7 1.0
OD2 B:ASP327 2.2 42.4 1.0
NE2 B:HIS331 2.3 37.8 1.0
OD1 B:ASP327 2.3 21.8 1.0
CG B:ASP327 2.6 36.7 1.0
NE2 B:HIS412 2.6 39.7 1.0
CD2 B:HIS412 3.1 37.5 1.0
P B:PO4453 3.1 68.7 1.0
CE1 B:HIS331 3.1 38.3 1.0
O3 B:PO4453 3.2 72.4 1.0
CD2 B:HIS331 3.3 36.0 1.0
HE2 B:HIS372 3.4 0.0 1.0
HG B:SER102 3.6 0.0 1.0
CE1 B:HIS370 3.7 15.1 1.0
CE1 B:HIS412 3.7 44.4 1.0
O2 B:PO4453 3.8 65.2 1.0
OG B:SER102 3.8 30.2 1.0
NE2 B:HIS370 3.8 16.6 1.0
NE2 B:HIS372 3.9 28.6 1.0
CB B:ASP327 4.1 37.4 1.0
ND1 B:HIS331 4.3 36.9 1.0
O4 B:PO4453 4.3 73.1 1.0
CG B:HIS331 4.3 37.5 1.0
CG B:HIS412 4.4 33.9 1.0
OD1 B:ASP51 4.4 39.9 1.0
CE1 B:HIS372 4.5 29.5 1.0
CD2 B:HIS372 4.6 19.9 1.0
ND1 B:HIS412 4.6 39.7 1.0
HD21 B:ASN369 4.7 0.0 1.0
H B:SER102 4.7 0.0 1.0
O B:ASP327 4.8 40.0 1.0
ND1 B:HIS370 4.9 14.6 1.0
C B:ASP327 4.9 41.0 1.0
CA B:ASP327 5.0 39.0 1.0

Reference:

T.T.Tibbitts, X.Xu, E.R.Kantrowitz. Kinetics and Crystal Structure of A Mutant Escherichia Coli Alkaline Phosphatase (Asp-369-->Asn): A Mechanism Involving One Zinc Per Active Site. Protein Sci. V. 3 2005 1994.
ISSN: ISSN 0961-8368
PubMed: 7703848
Page generated: Sat Oct 12 22:07:50 2024

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