Zinc in PDB 7y1s: Crystal Structure of Apo Leucyl Aminopeptidase From Bacillus Amyloliquefaciens

Enzymatic activity of Crystal Structure of Apo Leucyl Aminopeptidase From Bacillus Amyloliquefaciens

All present enzymatic activity of Crystal Structure of Apo Leucyl Aminopeptidase From Bacillus Amyloliquefaciens:
3.4.11.1;

Protein crystallography data

The structure of Crystal Structure of Apo Leucyl Aminopeptidase From Bacillus Amyloliquefaciens, PDB code: 7y1s was solved by P.Huang, Z.Q.Jiang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.87 / 2.75
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 200.245, 200.245, 89.022, 90, 90, 120
R / Rfree (%) 17 / 21.2

Other elements in 7y1s:

The structure of Crystal Structure of Apo Leucyl Aminopeptidase From Bacillus Amyloliquefaciens also contains other interesting chemical elements:

Nickel (Ni) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Apo Leucyl Aminopeptidase From Bacillus Amyloliquefaciens (pdb code 7y1s). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Apo Leucyl Aminopeptidase From Bacillus Amyloliquefaciens, PDB code: 7y1s:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 7y1s

Go back to Zinc Binding Sites List in 7y1s
Zinc binding site 1 out of 2 in the Crystal Structure of Apo Leucyl Aminopeptidase From Bacillus Amyloliquefaciens


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Apo Leucyl Aminopeptidase From Bacillus Amyloliquefaciens within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn503

b:90.4
occ:1.00
OD1 A:ASP343 2.1 71.1 1.0
OE1 A:GLU345 2.1 66.9 1.0
OD2 A:ASP266 2.1 72.4 1.0
O A:ASP343 2.2 58.9 1.0
CG A:ASP266 3.0 42.9 1.0
ZN A:ZN504 3.0 56.1 1.0
CD A:GLU345 3.0 50.0 1.0
CG A:ASP343 3.1 59.9 1.0
C A:ASP343 3.1 43.5 1.0
OD1 A:ASP266 3.2 46.0 1.0
OE2 A:GLU345 3.3 52.8 1.0
CA A:ASP343 3.6 44.5 1.0
CB A:ASP343 3.9 47.9 1.0
OD2 A:ASP343 3.9 54.6 1.0
O2 A:CO3501 4.1 52.4 1.0
N A:ALA344 4.3 43.0 1.0
N A:GLU345 4.3 47.5 1.0
CG A:GLU345 4.4 50.6 1.0
CB A:ASP266 4.4 49.3 1.0
CE A:LYS273 4.5 62.9 1.0
OD2 A:ASP284 4.6 50.5 1.0
ND2 A:ASN316 4.7 58.3 1.0
NZ A:LYS261 4.7 57.5 1.0
NZ A:LYS273 4.8 72.6 1.0
CB A:GLU345 4.8 51.0 1.0
CA A:ALA344 4.8 44.5 1.0
CA A:GLY268 4.9 34.9 1.0
O A:THR342 4.9 49.9 1.0
N A:ASP343 4.9 46.5 1.0

Zinc binding site 2 out of 2 in 7y1s

Go back to Zinc Binding Sites List in 7y1s
Zinc binding site 2 out of 2 in the Crystal Structure of Apo Leucyl Aminopeptidase From Bacillus Amyloliquefaciens


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Apo Leucyl Aminopeptidase From Bacillus Amyloliquefaciens within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn504

b:56.1
occ:1.00
OD2 A:ASP284 2.0 50.5 1.0
NZ A:LYS261 2.1 57.5 1.0
OE2 A:GLU345 2.1 52.8 1.0
OD2 A:ASP266 2.2 72.4 1.0
CG A:ASP284 3.0 59.1 1.0
ZN A:ZN503 3.0 90.4 1.0
CD A:GLU345 3.1 50.0 1.0
CE A:LYS261 3.2 45.8 1.0
OE1 A:GLU345 3.3 66.9 1.0
OD1 A:ASP284 3.3 72.1 1.0
CG A:ASP266 3.4 42.9 1.0
O2 A:CO3501 3.9 52.4 1.0
CB A:ASP266 4.0 49.3 1.0
O A:THR370 4.3 46.3 1.0
CB A:ASP284 4.3 47.6 1.0
OD1 A:ASP266 4.3 46.0 1.0
CG A:GLU345 4.5 50.6 1.0
CD A:LYS261 4.5 44.7 1.0
O A:ASP343 4.6 58.9 1.0
N A:GLY346 4.7 43.1 1.0
CG2 A:ILE263 4.8 48.3 1.0
CA A:GLY346 4.8 44.5 1.0
CB A:ILE263 4.9 48.1 1.0
O A:HOH636 4.9 57.4 1.0
CG1 A:ILE263 4.9 43.4 1.0
OD1 A:ASP343 4.9 71.1 1.0

Reference:

P.Huang, Z.Q.Jiang. Crystal Structure of Apo Leucyl Aminopeptidase From Bacillus Amyloliquefaciens To Be Published.
Page generated: Wed Oct 30 15:26:03 2024

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