Atomistry » Zinc » PDB 1h71-1hld » 1h71
Atomistry »
  Zinc »
    PDB 1h71-1hld »
      1h71 »

Zinc in PDB 1h71: Psychrophilic Protease From Pseudoalteromonas 'Tac II 18'

Enzymatic activity of Psychrophilic Protease From Pseudoalteromonas 'Tac II 18'

All present enzymatic activity of Psychrophilic Protease From Pseudoalteromonas 'Tac II 18':
3.4.24.40;

Protein crystallography data

The structure of Psychrophilic Protease From Pseudoalteromonas 'Tac II 18', PDB code: 1h71 was solved by V.Villeret, F.Van Petegem, N.Aghajari, J.-P.Chessa, C.Gerday, R.Haser, J.Van Beeumen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.000, 57.550, 161.810, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / 22.1

Other elements in 1h71:

The structure of Psychrophilic Protease From Pseudoalteromonas 'Tac II 18' also contains other interesting chemical elements:

Calcium (Ca) 8 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Psychrophilic Protease From Pseudoalteromonas 'Tac II 18' (pdb code 1h71). 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 Psychrophilic Protease From Pseudoalteromonas 'Tac II 18', PDB code: 1h71:

Zinc binding site 1 out of 1 in 1h71

Go back to Zinc Binding Sites List in 1h71
Zinc binding site 1 out of 1 in the Psychrophilic Protease From Pseudoalteromonas 'Tac II 18'


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Psychrophilic Protease From Pseudoalteromonas 'Tac II 18' within 5.0Å range:
probe atom residue distance (Å) B Occ
P:Zn600

b:28.6
occ:1.00
NE2 P:HIS173 2.2 19.4 1.0
O P:HOH2284 2.3 26.5 1.0
NE2 P:HIS179 2.3 27.3 1.0
NE2 P:HIS169 2.3 23.5 1.0
OH P:TYR209 3.0 33.9 0.5
CD2 P:HIS179 3.1 26.3 1.0
CD2 P:HIS169 3.1 24.2 1.0
CE1 P:HIS173 3.1 18.7 1.0
CD2 P:HIS173 3.2 20.7 1.0
CE1 P:HIS169 3.2 21.4 1.0
CE1 P:HIS179 3.2 30.4 1.0
CZ P:TYR209 3.7 33.3 0.5
OE2 P:GLU170 3.9 25.3 1.0
CE1 P:TYR209 4.2 43.2 0.5
O P:HOH2089 4.2 34.5 1.0
ND1 P:HIS173 4.2 20.4 1.0
ND1 P:HIS179 4.2 28.6 1.0
CE2 P:TYR209 4.2 32.5 0.5
CG P:HIS179 4.3 25.4 1.0
ND1 P:HIS169 4.3 21.4 1.0
O P:HOH2088 4.3 49.5 1.0
CG P:HIS173 4.3 21.6 1.0
CG P:HIS169 4.3 23.7 1.0
O P:HOH2121 4.4 34.8 1.0
OE1 P:GLU170 4.4 26.7 1.0
CE1 P:TYR209 4.5 34.6 0.5
CD P:GLU170 4.6 27.1 1.0
OH P:TYR209 4.7 45.0 0.5
CZ P:TYR209 4.8 43.6 0.5
CE P:MET207 4.9 21.0 1.0
CD1 P:TYR209 4.9 42.4 0.5

Reference:

N.Aghajari, F.Van Petegem, V.Villeret, J.-P.Chessa, C.Gerday, R.Haser, J.Van Beeumen. Crystal Structures of A Psychrophilic Metalloprotease Reveal New Insights Into Catalysis By Cold-Adapted Proteases Proteins: Struct.,Funct., V. 50 636 2003GENET..
ISSN: ISSN 0887-3585
PubMed: 12577270
DOI: 10.1002/PROT.10264
Page generated: Thu Oct 29 07:21:14 2020
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy