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Zinc in PDB 1lok: The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica Complexed with Tris: A Tale of Buffer Inhibition

Enzymatic activity of The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica Complexed with Tris: A Tale of Buffer Inhibition

All present enzymatic activity of The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica Complexed with Tris: A Tale of Buffer Inhibition:
3.4.11.10;

Protein crystallography data

The structure of The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica Complexed with Tris: A Tale of Buffer Inhibition, PDB code: 1lok was solved by W.T.Desmarais, D.L.Bienvenue, K.P.Bzymek, R.C.Holz, G.A.Petsko, D.Ringe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.08 / 1.20
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 108.338, 108.338, 93.519, 90.00, 90.00, 120.00
R / Rfree (%) 15.8 / 19.8

Other elements in 1lok:

The structure of The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica Complexed with Tris: A Tale of Buffer Inhibition also contains other interesting chemical elements:

Sodium (Na) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica Complexed with Tris: A Tale of Buffer Inhibition (pdb code 1lok). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica Complexed with Tris: A Tale of Buffer Inhibition, PDB code: 1lok:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1lok

Go back to Zinc Binding Sites List in 1lok
Zinc binding site 1 out of 2 in the The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica Complexed with Tris: A Tale of Buffer Inhibition


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica Complexed with Tris: A Tale of Buffer Inhibition within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn901

b:10.5
occ:1.00
OD2 A:ASP117 2.0 9.5 1.0
NE2 A:HIS256 2.1 11.9 1.0
OE2 A:GLU152 2.1 11.4 1.0
N A:TRS800 2.1 14.3 1.0
O1 A:TRS800 2.2 11.9 1.0
OE1 A:GLU152 2.4 12.8 1.0
CD A:GLU152 2.6 11.4 1.0
CG A:ASP117 2.9 9.2 1.0
C A:TRS800 3.0 14.4 1.0
C1 A:TRS800 3.0 13.3 1.0
CE1 A:HIS256 3.0 14.4 1.0
CD2 A:HIS256 3.1 11.3 1.0
OD1 A:ASP117 3.3 9.1 1.0
C2 A:TRS800 3.4 16.4 1.0
ZN A:ZN902 3.5 8.7 1.0
O2 A:TRS800 3.5 23.2 1.0
CG A:GLU152 4.1 12.2 1.0
ND1 A:HIS256 4.2 14.8 1.0
OE1 A:GLU151 4.2 12.4 1.0
O A:HOH1004 4.2 11.0 1.0
O A:HOH1051 4.2 22.5 1.0
CG A:HIS256 4.3 10.6 1.0
CB A:ASP117 4.3 8.8 1.0
C3 A:TRS800 4.4 16.4 1.0
O A:HOH1177 4.5 48.4 1.0
CD1 A:ILE255 4.6 15.1 1.0
NE2 A:HIS97 4.6 8.9 1.0
CE1 A:HIS97 4.7 9.0 1.0
O3 A:TRS800 4.7 17.0 1.0

Zinc binding site 2 out of 2 in 1lok

Go back to Zinc Binding Sites List in 1lok
Zinc binding site 2 out of 2 in the The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica Complexed with Tris: A Tale of Buffer Inhibition


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica Complexed with Tris: A Tale of Buffer Inhibition within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn902

b:8.7
occ:1.00
O1 A:TRS800 2.0 11.9 1.0
OD1 A:ASP117 2.0 9.1 1.0
NE2 A:HIS97 2.0 8.9 1.0
OD1 A:ASP179 2.1 11.4 1.0
O2 A:TRS800 2.2 23.2 1.0
OD2 A:ASP179 2.3 11.1 1.0
CG A:ASP179 2.5 10.2 1.0
C1 A:TRS800 2.9 13.3 1.0
CG A:ASP117 3.0 9.2 1.0
CE1 A:HIS97 3.0 9.0 1.0
CD2 A:HIS97 3.1 8.2 1.0
OD2 A:ASP117 3.4 9.5 1.0
C2 A:TRS800 3.5 16.4 1.0
ZN A:ZN901 3.5 10.5 1.0
OE1 A:GLU151 3.5 12.4 1.0
OE2 A:GLU152 3.7 11.4 1.0
C A:TRS800 3.7 14.4 1.0
CB A:ASP118 4.0 8.7 1.0
CB A:ASP179 4.1 11.2 1.0
ND1 A:HIS97 4.1 9.1 1.0
CD A:GLU151 4.2 12.1 1.0
O A:HOH1293 4.2 49.3 1.0
N A:TRS800 4.2 14.3 1.0
CG A:HIS97 4.2 8.0 1.0
CB A:ASP117 4.3 8.8 1.0
CD A:GLU152 4.4 11.4 1.0
CA A:ASP117 4.5 8.3 1.0
OE2 A:GLU151 4.5 16.5 1.0
CG A:ASP118 4.7 7.9 1.0
OE1 A:GLU152 4.7 12.8 1.0
C A:ASP117 4.7 8.4 1.0
CA A:ASP179 4.8 9.3 1.0
OG A:SER228 4.8 11.8 1.0
N A:ASP118 4.8 8.0 1.0
CG A:MET180 4.9 10.7 1.0
CA A:ASP118 4.9 7.8 1.0
OD2 A:ASP118 4.9 8.6 1.0
C A:ASP179 5.0 10.5 1.0

Reference:

W.T.Desmarais, D.L.Bienvenue, K.P.Bzymek, R.C.Holz, G.A.Petsko, D.Ringe. The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica Complexed with Tris A Tale of Buffer Inhibition Structure V. 10 1063 2002.
ISSN: ISSN 0969-2126
PubMed: 12176384
DOI: 10.1016/S0969-2126(02)00810-9
Page generated: Wed Dec 16 02:56:25 2020

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