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

Zinc in PDB 1atl: Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Form-D)

Enzymatic activity of Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Form-D)

All present enzymatic activity of Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Form-D):
3.4.24.42;

Protein crystallography data

The structure of Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Form-D), PDB code: 1atl was solved by D.Zhang, I.Botos, F.-X.Gomis-Rueth, R.Doll, C.Blood, F.G.Njoroge, J.W.Fox, W.Bode, E.F.Meyer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.80
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 97.320, 97.320, 87.760, 90.00, 90.00, 120.00
R / Rfree (%) 16 / n/a

Other elements in 1atl:

The structure of Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Form-D) also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Form-D) (pdb code 1atl). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Form-D), PDB code: 1atl:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1atl

Go back to Zinc Binding Sites List in 1atl
Zinc binding site 1 out of 2 in the Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Form-D)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Form-D) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:14.2
occ:1.00
 NE2 A:HIS142 2.0 5.7 1.0
NE2 A:HIS152 2.0 22.9 1.0
NE2 A:HIS146 2.1 14.8 1.0
OXT A:0QI301 2.1 39.3 0.8
O A:0QI301 2.2 19.7 0.8
C A:0QI301 2.4 39.0 0.8
CD2 A:HIS142 3.0 6.1 1.0
CE1 A:HIS152 3.0 16.6 1.0
CD2 A:HIS146 3.1 10.7 1.0
CE1 A:HIS142 3.1 6.0 1.0
CD2 A:HIS152 3.1 13.0 1.0
CE1 A:HIS146 3.1 12.3 1.0
CA A:0QI301 3.9 34.0 0.8
CG A:HIS142 4.2 6.3 1.0
ND1 A:HIS152 4.2 20.1 1.0
ND1 A:HIS142 4.2 6.2 1.0
CG A:HIS152 4.2 10.2 1.0
ND1 A:HIS146 4.2 20.7 1.0
CG A:HIS146 4.2 14.6 1.0
CD1 A:0QI301 4.3 32.5 0.8
CB A:0QI301 4.4 39.4 0.8
OE2 A:GLU143 4.5 14.4 1.0
CG A:0QI301 4.5 27.0 0.8
N A:0QI301 4.6 35.0 0.8
OE1 A:GLU143 4.6 16.1 1.0
CE A:MET166 4.6 9.5 1.0
CD A:GLU143 5.0 12.8 1.0

Zinc binding site 2 out of 2 in 1atl

Go back to Zinc Binding Sites List in 1atl
Zinc binding site 2 out of 2 in the Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Form-D)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Form-D) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn402

b:15.6
occ:1.00
 NE2 B:HIS152 2.0 9.9 1.0
NE2 B:HIS142 2.0 10.3 1.0
NE2 B:HIS146 2.1 15.6 1.0
OXT B:0QI311 2.1 34.6 0.8
O B:0QI311 2.2 25.7 0.8
C B:0QI311 2.4 8.2 0.8
CE1 B:HIS152 3.0 13.9 1.0
CD2 B:HIS142 3.0 5.4 1.0
CD2 B:HIS152 3.1 12.3 1.0
CE1 B:HIS146 3.1 11.3 1.0
CD2 B:HIS146 3.1 5.0 1.0
CE1 B:HIS142 3.1 9.0 1.0
CA B:0QI311 3.9 17.0 0.8
ND1 B:HIS152 4.1 10.1 1.0
CG B:HIS152 4.2 12.4 1.0
CG B:HIS142 4.2 6.4 1.0
ND1 B:HIS146 4.2 10.3 1.0
ND1 B:HIS142 4.2 14.0 1.0
CG B:HIS146 4.2 16.7 1.0
CD1 B:0QI311 4.3 28.4 0.8
CB B:0QI311 4.4 36.1 0.8
OE2 B:GLU143 4.5 16.2 1.0
O B:HOH951 4.6 45.4 1.0
CG B:0QI311 4.6 17.9 0.8
N B:0QI311 4.6 40.1 0.8
CE B:MET166 4.7 6.8 1.0
OE1 B:GLU143 4.7 11.7 1.0
O B:HOH920 4.7 43.0 1.0

Reference:

D.Zhang, I.Botos, F.X.Gomis-Ruth, R.Doll, C.Blood, F.G.Njoroge, J.W.Fox, W.Bode, E.F.Meyer. Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Form D). Proc.Natl.Acad.Sci.Usa V. 91 8447 1994.
ISSN: ISSN 0027-8424
PubMed: 8078901
DOI: 10.1073/PNAS.91.18.8447
Page generated: Sat Oct 12 22:16:31 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy