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Chlorine in PDB 7stt: Crystal Structure of Sulfatase From Pedobacter Yulinensis

Protein crystallography data

The structure of Crystal Structure of Sulfatase From Pedobacter Yulinensis, PDB code: 7stt was solved by A.O'malley, C.R.Schlachter, L.L.Grimes, J.J.Tomashek, A.L.Lee, M.Chruszcz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.37 / 1.60
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 83.62, 83.62, 116.052, 90, 90, 120
R / Rfree (%) 14.8 / 17.8

Other elements in 7stt:

The structure of Crystal Structure of Sulfatase From Pedobacter Yulinensis also contains other interesting chemical elements:

Calcium (Ca) 1 atom
Sodium (Na) 3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Sulfatase From Pedobacter Yulinensis (pdb code 7stt). 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 Crystal Structure of Sulfatase From Pedobacter Yulinensis, PDB code: 7stt:

Chlorine binding site 1 out of 1 in 7stt

Go back to Chlorine Binding Sites List in 7stt
Chlorine binding site 1 out of 1 in the Crystal Structure of Sulfatase From Pedobacter Yulinensis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Sulfatase From Pedobacter Yulinensis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl505

b:27.3
occ:1.00
NE A:ARG378 3.3 14.5 1.0
NH2 A:ARG378 3.3 18.4 1.0
ND2 A:ASN377 3.6 20.9 1.0
CZ A:ARG378 3.7 16.1 1.0
CB A:ASN377 3.8 16.1 1.0
CZ2 A:TRP295 4.1 16.4 1.0
CG A:ARG378 4.2 13.0 1.0
CG A:ASN377 4.2 17.4 1.0
CD A:ARG378 4.4 13.5 1.0
CH2 A:TRP295 4.4 17.9 1.0
CA A:ASN377 4.9 14.3 1.0

Reference:

C.R.Schlachter, A.O'malley, L.L.Grimes, J.J.Tomashek, M.Chruszcz, L.A.Lee. Purification, Characterization, and Structural Studies of A Sulfatase From Pedobacter Yulinensis . Molecules V. 27 2021.
ISSN: ESSN 1420-3049
PubMed: 35011319
DOI: 10.3390/MOLECULES27010087
Page generated: Sun Jul 13 07:11:09 2025

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