Chlorine in PDB 3irt: Crystal Structure of the I93M Mutant of Ubiquitin Carboxy-Terminal Hydrolase L1

All present enzymatic activity of Crystal Structure of the I93M Mutant of Ubiquitin Carboxy-Terminal Hydrolase L1:
3.4.19.12;

The structure of Crystal Structure of the I93M Mutant of Ubiquitin Carboxy-Terminal Hydrolase L1, PDB code: 3irt was solved by C.W.Davies, T.K.Maiti, C.Das, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.75 / 2.80
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	109.938, 109.938, 79.040, 90.00, 90.00, 90.00
R / Rfree (%)	21.1 / 25.4

The binding sites of Chlorine atom in the Crystal Structure of the I93M Mutant of Ubiquitin Carboxy-Terminal Hydrolase L1 (pdb code 3irt). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the I93M Mutant of Ubiquitin Carboxy-Terminal Hydrolase L1, PDB code: 3irt:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of the I93M Mutant of Ubiquitin Carboxy-Terminal Hydrolase L1


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 the I93M Mutant of Ubiquitin Carboxy-Terminal Hydrolase L1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl224 b:79.2 occ:1.00 CB A:CYS90 3.0 65.3 1.0 NE2 A:GLN84 3.2 52.8 1.0 CA A:CYS90 3.8 58.0 1.0 N A:ASN88 3.8 57.7 1.0 N A:CYS90 3.8 51.4 1.0 SG A:CYS90 3.9 70.1 1.0 NH1 A:ARG178 4.2 71.8 1.0 CA A:ASN88 4.2 57.7 1.0 CD A:GLN84 4.3 57.8 1.0 O A:PHE160 4.6 51.7 1.0 C A:ASN88 4.6 53.2 1.0 OE1 A:GLN84 4.6 52.9 1.0 N A:SER89 4.7 50.5 1.0 C A:GLY87 4.9 56.0 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of the I93M Mutant of Ubiquitin Carboxy-Terminal Hydrolase L1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the I93M Mutant of Ubiquitin Carboxy-Terminal Hydrolase L1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl224 b:86.6 occ:1.00 CB B:CYS90 2.9 67.6 1.0 N B:ASN88 3.5 57.0 1.0 NE2 B:GLN84 3.5 55.0 1.0 N B:CYS90 3.7 47.0 1.0 CA B:CYS90 3.7 58.8 1.0 CA B:ASN88 3.7 59.1 1.0 SG B:CYS90 3.9 70.3 1.0 C B:ASN88 4.2 54.4 1.0 N B:SER89 4.4 55.5 1.0 C B:GLY87 4.6 56.4 1.0 CD B:GLN84 4.7 56.4 1.0 NH1 B:ARG178 4.7 68.4 1.0 OD1 B:ASN88 4.9 67.0 1.0 C B:SER89 4.9 47.9 1.0 O B:PHE160 4.9 49.4 1.0 O B:ASN88 4.9 49.0 1.0 CA B:GLY87 5.0 63.0 1.0

D.A.Boudreaux, T.K.Maiti, C.W.Davies, C.Das. Ubiquitin Vinyl Methyl Ester Binding Orients the Misaligned Active Site of the Ubiquitin Hydrolase UCHL1 Into Productive Conformation. Proc.Natl.Acad.Sci.Usa V. 107 9117 2010.
ISSN: ISSN 0027-8424
PubMed: 20439756
DOI: 10.1073/PNAS.0910870107