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Chlorine in PDB 255l: Hydrolase

Enzymatic activity of Hydrolase

All present enzymatic activity of Hydrolase:
3.2.1.17;

Protein crystallography data

The structure of Hydrolase, PDB code: 255l was solved by R.Kuroki, B.Shoichet, L.H.Weaver, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.80
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 61.200, 61.200, 97.000, 90.00, 90.00, 120.00
R / Rfree (%) 16 / n/a

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Hydrolase (pdb code 255l). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Hydrolase, PDB code: 255l:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 255l

Go back to Chlorine Binding Sites List in 255l
Chlorine binding site 1 out of 2 in the Hydrolase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Hydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl173

b:3.2
occ:1.00
O A:HOH209 2.8 30.6 1.0
N A:ARG145 3.2 11.1 1.0
N A:ASN144 3.4 4.9 1.0
C A:THR142 3.5 18.1 1.0
CA A:THR142 3.5 9.6 1.0
CB A:THR142 3.5 15.2 1.0
O A:THR142 3.7 14.8 1.0
CB A:ASN144 3.7 12.9 1.0
CB A:ARG145 3.8 13.5 1.0
CA A:ASN144 3.9 10.3 1.0
N A:PRO143 3.9 14.2 1.0
C A:ASN144 4.0 15.7 1.0
CA A:ARG145 4.1 12.3 1.0
CG2 A:THR142 4.2 15.7 1.0
C A:PRO143 4.3 13.4 1.0
CD A:PRO143 4.3 14.2 1.0
CA A:PRO143 4.7 13.2 1.0
CG A:ASN144 4.7 32.1 1.0
OG1 A:THR142 4.7 16.8 1.0
O A:HOH230 4.8 42.0 1.0
ND2 A:ASN144 4.9 34.0 1.0
N A:THR142 5.0 12.4 1.0

Chlorine binding site 2 out of 2 in 255l

Go back to Chlorine Binding Sites List in 255l
Chlorine binding site 2 out of 2 in the Hydrolase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Hydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl178

b:5.5
occ:0.50
O A:HOH215 2.8 22.5 1.0
O A:HOH182 3.2 22.9 1.0
O A:HOH200 3.4 30.1 1.0
O A:HOH246 3.8 53.0 1.0
CB A:ALA49 4.0 16.5 1.0
CE1 A:HIS31 4.1 14.6 1.0
NE2 A:HIS31 4.2 11.5 1.0
NE2 A:GLN69 4.2 15.2 1.0
CA A:ALA49 4.4 18.8 1.0
O A:HOH282 4.5 36.1 1.0
CD2 A:LEU66 4.5 21.0 1.0
O A:HOH202 4.8 55.1 1.0
O A:ALA49 4.9 13.6 1.0

Reference:

B.K.Shoichet, W.A.Baase, R.Kuroki, B.W.Matthews. A Relationship Between Protein Stability and Protein Function. Proc.Natl.Acad.Sci.Usa V. 92 452 1995.
ISSN: ISSN 0027-8424
PubMed: 7831309
DOI: 10.1073/PNAS.92.2.452
Page generated: Sat Dec 12 08:58:05 2020

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