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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

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