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Zinc in PDB 1ast: Structure of Astacin and Implications For Activation of Astacins and Zinc-Ligation of Collagenases

Enzymatic activity of Structure of Astacin and Implications For Activation of Astacins and Zinc-Ligation of Collagenases

All present enzymatic activity of Structure of Astacin and Implications For Activation of Astacins and Zinc-Ligation of Collagenases:
3.4.24.21;

Protein crystallography data

The structure of Structure of Astacin and Implications For Activation of Astacins and Zinc-Ligation of Collagenases, PDB code: 1ast was solved by W.Bode, F.X.Gomis-Rueth, W.Stoecker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.80
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 61.960, 61.960, 98.520, 90.00, 90.00, 120.00
R / Rfree (%) 15.8 / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Astacin and Implications For Activation of Astacins and Zinc-Ligation of Collagenases (pdb code 1ast). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of Astacin and Implications For Activation of Astacins and Zinc-Ligation of Collagenases, PDB code: 1ast:

Zinc binding site 1 out of 1 in 1ast

Go back to Zinc Binding Sites List in 1ast
Zinc binding site 1 out of 1 in the Structure of Astacin and Implications For Activation of Astacins and Zinc-Ligation of Collagenases


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Astacin and Implications For Activation of Astacins and Zinc-Ligation of Collagenases within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn999

b:10.4
occ:1.00
 O A:HOH300 2.0 9.9 1.0
NE2 A:HIS102 2.0 6.0 1.0
NE2 A:HIS92 2.0 5.4 1.0
NE2 A:HIS96 2.2 4.7 1.0
OH A:TYR149 2.5 10.1 1.0
CE1 A:HIS92 3.0 5.5 1.0
CD2 A:HIS102 3.0 3.5 1.0
CE1 A:HIS102 3.0 10.5 1.0
CD2 A:HIS92 3.0 5.3 1.0
CD2 A:HIS96 3.1 3.5 1.0
CE1 A:HIS96 3.3 4.3 1.0
CZ A:TYR149 3.4 10.5 1.0
CE1 A:TYR149 3.9 9.1 1.0
O A:HOH357 3.9 19.2 1.0
O A:HOH328 4.0 23.5 1.0
ND1 A:HIS92 4.1 6.0 1.0
ND1 A:HIS102 4.2 12.1 1.0
OE1 A:GLU93 4.2 15.8 1.0
CG A:HIS102 4.2 10.6 1.0
CG A:HIS92 4.2 2.9 1.0
O A:HOH330 4.2 21.2 1.0
OE2 A:GLU93 4.2 18.1 1.0
CE2 A:TYR149 4.3 9.4 1.0
CG A:HIS96 4.3 5.5 1.0
ND1 A:HIS96 4.3 7.4 1.0
CD A:GLU93 4.6 11.4 1.0
CE A:MET147 4.8 5.5 1.0

Reference:

W.Bode, F.X.Gomis-Ruth, R.Huber, R.Zwilling, W.Stocker. Structure of Astacin and Implications For Activation of Astacins and Zinc-Ligation of Collagenases. Nature V. 358 164 1992.
ISSN: ISSN 0028-0836
PubMed: 1319561
DOI: 10.1038/358164A0
Page generated: Sat Oct 12 22:15:41 2024

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