Zinc in PDB 3hwp: Crystal Structure and Computational Analyses Provide Insights Into the Catalytic Mechanism of 2, 4-Diacetylphloroglucinol Hydrolase Phlg From Pseudomonas Fluorescens

The structure of Crystal Structure and Computational Analyses Provide Insights Into the Catalytic Mechanism of 2, 4-Diacetylphloroglucinol Hydrolase Phlg From Pseudomonas Fluorescens, PDB code: 3hwp was solved by Y.-X.He, L.Huang, Y.Xue, X.Fei, Y.-B.Teng, C.-Z.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.99 / 2.00
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	124.785, 132.612, 95.059, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 21.7

The structure of Crystal Structure and Computational Analyses Provide Insights Into the Catalytic Mechanism of 2, 4-Diacetylphloroglucinol Hydrolase Phlg From Pseudomonas Fluorescens also contains other interesting chemical elements:

Nickel	(Ni)	1 atom
Chlorine	(Cl)	1 atom

The binding sites of Zinc atom in the Crystal Structure and Computational Analyses Provide Insights Into the Catalytic Mechanism of 2, 4-Diacetylphloroglucinol Hydrolase Phlg From Pseudomonas Fluorescens (pdb code 3hwp). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure and Computational Analyses Provide Insights Into the Catalytic Mechanism of 2, 4-Diacetylphloroglucinol Hydrolase Phlg From Pseudomonas Fluorescens, PDB code: 3hwp:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure and Computational Analyses Provide Insights Into the Catalytic Mechanism of 2, 4-Diacetylphloroglucinol Hydrolase Phlg From Pseudomonas Fluorescens


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure and Computational Analyses Provide Insights Into the Catalytic Mechanism of 2, 4-Diacetylphloroglucinol Hydrolase Phlg From Pseudomonas Fluorescens within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn295 b:21.8 occ:1.00 NE2 A:HIS129 2.1 20.6 1.0 OE1 A:GLU274 2.1 18.3 1.0 NE2 A:HIS270 2.2 21.5 1.0 OE1 A:GLU160 2.2 22.8 1.0 O A:HOH307 2.3 27.4 1.0 CD A:GLU274 3.0 20.6 1.0 CE1 A:HIS129 3.0 21.5 1.0 CD2 A:HIS129 3.1 22.0 1.0 CD2 A:HIS270 3.1 19.2 1.0 CE1 A:HIS270 3.2 21.4 1.0 OE2 A:GLU274 3.3 24.2 1.0 CD A:GLU160 3.3 30.6 1.0 OE2 A:GLU160 3.8 38.3 1.0 ND1 A:HIS129 4.2 20.8 1.0 OH A:TYR121 4.2 28.0 1.0 CG A:HIS129 4.2 21.1 1.0 ND1 A:HIS270 4.3 19.4 1.0 CG A:HIS270 4.3 21.1 1.0 CG A:GLU274 4.4 15.6 1.0 CD1 A:PHE125 4.5 18.2 1.0 CG A:GLU160 4.6 22.4 1.0 CB A:GLU274 4.6 17.1 1.0 CB A:GLU160 4.8 23.0 1.0 CZ A:TYR121 5.0 25.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure and Computational Analyses Provide Insights Into the Catalytic Mechanism of 2, 4-Diacetylphloroglucinol Hydrolase Phlg From Pseudomonas Fluorescens


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure and Computational Analyses Provide Insights Into the Catalytic Mechanism of 2, 4-Diacetylphloroglucinol Hydrolase Phlg From Pseudomonas Fluorescens within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn295 b:22.8 occ:1.00 NE2 B:HIS129 2.1 22.5 1.0 O B:HOH297 2.1 24.9 1.0 OE1 B:GLU160 2.1 21.8 1.0 OE1 B:GLU274 2.1 21.1 1.0 NE2 B:HIS270 2.2 18.4 1.0 CD2 B:HIS129 3.0 22.5 1.0 CE1 B:HIS129 3.0 19.8 1.0 CD B:GLU274 3.1 25.2 1.0 CD2 B:HIS270 3.2 21.3 1.0 CE1 B:HIS270 3.2 21.4 1.0 CD B:GLU160 3.3 28.2 1.0 OE2 B:GLU274 3.5 27.6 1.0 OE2 B:GLU160 3.8 40.4 1.0 ND1 B:HIS129 4.2 19.3 1.0 CG B:HIS129 4.2 20.9 1.0 ND1 B:HIS270 4.3 19.4 1.0 OH B:TYR121 4.3 24.9 1.0 CG B:HIS270 4.3 21.2 1.0 CG B:GLU274 4.4 20.2 1.0 CG B:GLU160 4.5 24.7 1.0 CD1 B:PHE125 4.6 19.2 1.0 CB B:GLU274 4.7 18.0 1.0 CB B:GLU160 4.9 23.3 1.0 CB B:PHE125 5.0 19.7 1.0

Y.X.He, L.Huang, Y.Xue, X.Fei, Y.B.Teng, S.B.Rubin-Pitel, H.Zhao, C.Z.Zhou. Crystal Structure and Computational Analyses Provide Insights Into the Catalytic Mechanism of 2,4-Diacetylphloroglucinol Hydrolase Phlg From Pseudomonas Fluorescens. J.Biol.Chem. V. 285 4603 2010.
ISSN: ISSN 0021-9258
PubMed: 20018877
DOI: 10.1074/JBC.M109.044180