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Zinc in PDB 2zws: Crystal Structure Analysis of Neutral Ceramidase From Pseudomonas Aeruginosa

Enzymatic activity of Crystal Structure Analysis of Neutral Ceramidase From Pseudomonas Aeruginosa

All present enzymatic activity of Crystal Structure Analysis of Neutral Ceramidase From Pseudomonas Aeruginosa:
3.5.1.23;

Protein crystallography data

The structure of Crystal Structure Analysis of Neutral Ceramidase From Pseudomonas Aeruginosa, PDB code: 2zws was solved by Y.Kakuta, N.Okino, T.Inoue, H.Okano, M.Ito, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.60 / 1.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 182.175, 59.292, 70.976, 90.00, 102.16, 90.00
R / Rfree (%) 17.4 / 20.6

Other elements in 2zws:

The structure of Crystal Structure Analysis of Neutral Ceramidase From Pseudomonas Aeruginosa also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure Analysis of Neutral Ceramidase From Pseudomonas Aeruginosa (pdb code 2zws). 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 Analysis of Neutral Ceramidase From Pseudomonas Aeruginosa, PDB code: 2zws:

Zinc binding site 1 out of 1 in 2zws

Go back to Zinc Binding Sites List in 2zws
Zinc binding site 1 out of 1 in the Crystal Structure Analysis of Neutral Ceramidase From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure Analysis of Neutral Ceramidase From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn647

b:14.8
occ:1.00
 OE1 A:GLU411 2.1 12.2 1.0
NE2 A:HIS204 2.1 16.7 1.0
O A:HOH966 2.1 20.1 1.0
NE2 A:HIS97 2.2 13.7 1.0
OH A:TYR448 2.2 16.2 1.0
OE2 A:GLU411 2.5 14.3 1.0
CD A:GLU411 2.6 14.5 1.0
CD2 A:HIS204 3.0 13.0 1.0
CE1 A:HIS97 3.1 11.6 1.0
CE1 A:HIS204 3.1 13.4 1.0
CZ A:TYR448 3.2 13.7 1.0
CD2 A:HIS97 3.2 12.7 1.0
CE2 A:TYR448 3.8 15.1 1.0
O1 A:GOL656 3.8 33.2 1.0
O A:HOH1004 3.9 29.3 1.0
CG A:GLU411 4.1 15.2 1.0
CE1 A:TYR448 4.2 12.9 1.0
OH A:TYR441 4.2 14.8 1.0
CG A:HIS204 4.2 14.4 1.0
ND1 A:HIS204 4.2 14.3 1.0
NE2 A:HIS99 4.2 16.2 1.0
ND1 A:HIS97 4.3 12.2 1.0
CG A:HIS97 4.3 13.1 1.0
NH2 A:ARG160 4.3 15.8 1.0
O2 A:GOL656 4.3 37.0 1.0
CE1 A:HIS99 4.4 16.1 1.0
C2 A:GOL656 4.6 36.4 1.0
CE1 A:TYR441 4.6 14.1 1.0
C1 A:GOL656 4.7 36.8 1.0
NH1 A:ARG160 4.7 17.8 1.0
CB A:GLU411 4.8 14.6 1.0
OH A:TYR445 4.8 13.8 1.0
CZ A:TYR441 4.9 14.4 1.0
CZ A:ARG160 5.0 16.1 1.0

Reference:

T.Inoue, N.Okino, Y.Kakuta, A.Hijikata, H.Okano, H.M.Goda, M.Tani, N.Sueyoshi, K.Kambayashi, H.Matsumura, Y.Kai, M.Ito. Mechanistic Insights Into the Hydrolysis and Synthesis of Ceramide By Neutral Ceramidase. J.Biol.Chem. V. 284 9566 2009.
ISSN: ISSN 0021-9258
PubMed: 19088069
DOI: 10.1074/JBC.M808232200
Page generated: Thu Oct 24 10:56:13 2024

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