Chlorine in PDB 7pp3: Structure of Ester-Hydrolase EH7 From the Metagenome of Marine Sediments at Milazzo Harbor (Sicily, Italy)

Protein crystallography data

The structure of Structure of Ester-Hydrolase EH7 From the Metagenome of Marine Sediments at Milazzo Harbor (Sicily, Italy), PDB code: 7pp3 was solved by I.Cea-Rama, J.Sanz-Aparicio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.04 / 2.25
Space group P 43 2 2
Cell size a, b, c (Å), α, β, γ (°) 102.937, 102.937, 331.823, 90, 90, 90
R / Rfree (%) 18.7 / 22.7

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Ester-Hydrolase EH7 From the Metagenome of Marine Sediments at Milazzo Harbor (Sicily, Italy) (pdb code 7pp3). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structure of Ester-Hydrolase EH7 From the Metagenome of Marine Sediments at Milazzo Harbor (Sicily, Italy), PDB code: 7pp3:

Chlorine binding site 1 out of 1 in 7pp3

Go back to Chlorine Binding Sites List in 7pp3
Chlorine binding site 1 out of 1 in the Structure of Ester-Hydrolase EH7 From the Metagenome of Marine Sediments at Milazzo Harbor (Sicily, Italy)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Ester-Hydrolase EH7 From the Metagenome of Marine Sediments at Milazzo Harbor (Sicily, Italy) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl504

b:53.6
occ:1.00
O C:VAL408 4.1 48.5 1.0
CG2 C:ILE10 4.2 53.5 1.0
O C:HOH681 4.3 41.6 1.0
CA C:GLY13 4.3 40.5 1.0
OD1 C:ASP409 4.4 61.2 1.0
CA C:ASP409 4.6 56.5 1.0
C C:VAL408 4.6 46.1 1.0
N C:ASP409 4.7 50.2 1.0
CD1 C:ILE10 4.8 54.0 1.0
CG2 C:VAL408 4.9 49.2 1.0

Reference:

I.Cea-Rama, C.Coscolin, J.L.Gonzalez-Alfonso, J.Raj, M.Vasiljevic, F.J.Plou, M.Ferrer, J.Sanz-Aparicio. Crystal Structure of A Family VIII Beta-Lactamase Fold Hydrolase Reveals the Molecular Mechanism For Its Broad Substrate Scope. Febs J. V. 289 6714 2022.
ISSN: ISSN 1742-464X
PubMed: 35694902
DOI: 10.1111/FEBS.16554
Page generated: Tue Jul 30 02:35:48 2024

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