Chlorine in PDB 2etl: Crystal Structure of Ubiquitin Carboxy-Terminal Hydrolase L1 (Uch-L1)

All present enzymatic activity of Crystal Structure of Ubiquitin Carboxy-Terminal Hydrolase L1 (Uch-L1):
3.4.19.12;

The structure of Crystal Structure of Ubiquitin Carboxy-Terminal Hydrolase L1 (Uch-L1), PDB code: 2etl was solved by C.Das, Q.Q.Hoang, C.A.Kreinbring, S.J.Luchansky, R.K.Meray, S.S.Ray, P.T.Lansbury, D.Ringe, G.A.Petsko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.90 / 2.40
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.097, 110.097, 79.489, 90.00, 90.00, 90.00
R / Rfree (%)	22.3 / 27.4

The binding sites of Chlorine atom in the Crystal Structure of Ubiquitin Carboxy-Terminal Hydrolase L1 (Uch-L1) (pdb code 2etl). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of Ubiquitin Carboxy-Terminal Hydrolase L1 (Uch-L1), PDB code: 2etl:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of Ubiquitin Carboxy-Terminal Hydrolase L1 (Uch-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 Ubiquitin Carboxy-Terminal Hydrolase L1 (Uch-L1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl3003 b:38.4 occ:1.00 O A:HOH2049 3.3 40.4 1.0 NE2 A:GLN84 3.5 26.4 1.0 N A:ASN88 3.5 30.5 1.0 O A:HOH2003 3.6 22.7 1.0 CA A:ASN88 3.9 30.5 1.0 CB A:CYS90 4.0 30.8 1.0 SG A:CYS90 4.1 29.8 1.0 N A:SER89 4.3 27.7 1.0 N A:CYS90 4.3 27.9 1.0 C A:ASN88 4.5 29.2 1.0 CD A:GLN84 4.6 27.9 1.0 ND2 A:ASN88 4.6 29.8 1.0 C A:GLY87 4.6 30.9 1.0 OE1 A:GLN84 4.7 28.1 1.0 CA A:CYS90 4.8 28.2 1.0 NH1 A:ARG178 4.8 43.3 1.0 CA A:GLY87 4.9 31.4 1.0 O A:PHE160 4.9 23.2 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of Ubiquitin Carboxy-Terminal Hydrolase L1 (Uch-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 Ubiquitin Carboxy-Terminal Hydrolase L1 (Uch-L1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl3004 b:55.0 occ:1.00 N A:ASP169 3.3 29.7 1.0 CA A:ASP169 4.0 28.6 1.0 C A:VAL168 4.3 30.4 1.0 NZ A:LYS78 4.4 38.4 1.0 CA A:VAL168 4.4 31.0 1.0 CG1 A:VAL168 4.5 27.1 1.0 CE A:LYS78 4.8 39.1 1.0 CB A:ASP169 5.0 27.1 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of Ubiquitin Carboxy-Terminal Hydrolase L1 (Uch-L1)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Ubiquitin Carboxy-Terminal Hydrolase L1 (Uch-L1) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl3001 b:40.9 occ:1.00 N B:ASN88 3.1 40.0 1.0 NE2 B:GLN84 3.4 39.7 1.0 CA B:ASN88 3.6 39.6 1.0 O B:HOH2098 3.7 38.9 1.0 N B:SER89 3.9 35.4 1.0 SG B:CYS90 4.0 35.0 1.0 N B:CYS90 4.1 29.1 1.0 CB B:CYS90 4.1 29.3 1.0 C B:GLY87 4.1 42.9 1.0 C B:ASN88 4.2 37.3 1.0 CA B:GLY87 4.4 44.0 1.0 CD B:GLN84 4.5 41.5 1.0 OD1 B:ASN88 4.6 35.5 1.0 CA B:CYS90 4.7 29.3 1.0 OE1 B:GLN84 4.8 41.7 1.0 CB B:ASN88 5.0 39.0 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of Ubiquitin Carboxy-Terminal Hydrolase L1 (Uch-L1)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Ubiquitin Carboxy-Terminal Hydrolase L1 (Uch-L1) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl3002 b:73.0 occ:1.00 N B:ASP169 3.4 52.7 1.0 CA B:ASP169 3.9 53.8 1.0 C B:VAL168 4.5 51.3 1.0 CA B:VAL168 4.6 50.4 1.0 CG1 B:VAL168 4.7 51.9 1.0 CB B:ASP169 4.8 58.5 1.0 CD B:LYS78 4.9 58.1 1.0 OD2 B:ASP169 5.0 62.6 1.0

C.Das, Q.Q.Hoang, C.A.Kreinbring, S.J.Luchansky, R.K.Meray, S.S.Ray, P.T.Lansbury, D.Ringe, G.A.Petsko. Structural Basis For Conformational Plasticity of the Parkinson'S Disease-Associated Ubiquitin Hydrolase Uch-L1. Proc.Natl.Acad.Sci.Usa V. 103 4675 2006.
ISSN: ISSN 0027-8424
PubMed: 16537382
DOI: 10.1073/PNAS.0510403103