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Zinc in PDB 1omj: Crystal Structure of A Psychrophilic Alkaline Protease From Pseudomonas Tac II 18

Enzymatic activity of Crystal Structure of A Psychrophilic Alkaline Protease From Pseudomonas Tac II 18

All present enzymatic activity of Crystal Structure of A Psychrophilic Alkaline Protease From Pseudomonas Tac II 18:
3.4.24.40;

Protein crystallography data

The structure of Crystal Structure of A Psychrophilic Alkaline Protease From Pseudomonas Tac II 18, PDB code: 1omj was solved by S.Ravaud, P.Gouet, R.Haser, N.Aghajari, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.38
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 184.600, 184.600, 37.850, 90.00, 90.00, 120.00
R / Rfree (%) 19.5 / 24.6

Other elements in 1omj:

The structure of Crystal Structure of A Psychrophilic Alkaline Protease From Pseudomonas Tac II 18 also contains other interesting chemical elements:

Calcium (Ca) 8 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of A Psychrophilic Alkaline Protease From Pseudomonas Tac II 18 (pdb code 1omj). 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 Crystal Structure of A Psychrophilic Alkaline Protease From Pseudomonas Tac II 18, PDB code: 1omj:

Zinc binding site 1 out of 1 in 1omj

Go back to Zinc Binding Sites List in 1omj
Zinc binding site 1 out of 1 in the Crystal Structure of A Psychrophilic Alkaline Protease From Pseudomonas 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 Crystal Structure of A Psychrophilic Alkaline Protease From Pseudomonas Tac II 18 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn600

b:15.5
occ:1.00
 NE2 A:HIS179 2.2 18.7 1.0
NE2 A:HIS169 2.2 8.7 1.0
NE2 A:HIS173 2.2 12.1 1.0
O A:HOH1459 2.5 1.0 1.0
CE1 A:HIS169 3.1 11.6 1.0
CE1 A:HIS179 3.1 18.2 1.0
CD2 A:HIS179 3.1 18.6 1.0
CD2 A:HIS169 3.2 9.9 1.0
CD2 A:HIS173 3.2 10.1 1.0
CE1 A:HIS173 3.2 12.3 1.0
O A:HOH1029 4.1 21.1 1.0
CE1 A:TYR209 4.1 24.2 1.0
ND1 A:HIS169 4.2 12.2 1.0
ND1 A:HIS179 4.2 17.3 1.0
OH A:TYR209 4.3 29.1 1.0
CG A:HIS179 4.3 16.8 1.0
CG A:HIS169 4.3 10.5 1.0
ND1 A:HIS173 4.3 13.2 1.0
CG A:HIS173 4.3 11.3 1.0
O A:HOH2000 4.4 24.6 1.0
CE A:MET207 4.5 9.6 1.0
CZ A:TYR209 4.7 25.7 1.0
OE2 A:GLU170 4.8 16.6 1.0
O A:HOH1461 4.8 20.2 1.0
O A:HOH2001 5.0 16.4 1.0

Reference:

S.Ravaud, P.Gouet, R.Haser, N.Aghajari. Probing the Role of Divalent Metal Ions in A Bacterial Psychrophilic Metalloprotease: Binding Studies of An Enzyme in the Crystalline State By X-Ray Crystallography. J.Bacteriol. V. 185 4195 2003.
ISSN: ISSN 0021-9193
PubMed: 12837794
DOI: 10.1128/JB.185.14.4195-4203.2003
Page generated: Wed Oct 16 17:31:54 2024

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