Chlorine in PDB 1ba0: Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3

All present enzymatic activity of Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3:
3.6.1.3;

The structure of Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3, PDB code: 1ba0 was solved by S.M.Wilbanks, D.B.Mckay, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	143.300, 63.800, 46.500, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 27.5

The structure of Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3 also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Sodium	(Na)	1 atom

The binding sites of Chlorine atom in the Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3 (pdb code 1ba0). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3, PDB code: 1ba0:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl451 b:23.8 occ:1.00 O A:HOH892 3.1 66.8 1.0 CD1 A:TYR183 3.7 4.7 1.0 O A:TYR183 4.0 16.1 1.0 CA A:TYR183 4.2 12.8 1.0 O A:HOH893 4.2 39.5 1.0 CE1 A:TYR183 4.4 5.5 1.0 C A:TYR183 4.4 14.4 1.0 CG A:TYR183 4.5 9.2 1.0 CB A:TYR183 4.5 9.9 1.0 OG A:SER362 4.8 10.6 1.0 O A:HOH524 4.8 22.2 1.0 O A:ALA182 4.8 12.4 1.0

Chlorine binding site 2 out of 2 in the Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl455 b:12.5 occ:1.00 O A:HOH612 3.2 8.2 1.0 NZ A:LYS126 3.3 10.9 1.0 N A:ASP32 3.3 15.4 1.0 NE2 A:GLN33 3.3 9.4 1.0 CB A:ASN31 3.4 11.8 1.0 CB A:ASP32 3.6 17.4 1.0 CG A:ASP32 3.7 25.7 1.0 CD A:LYS126 3.7 7.8 1.0 CG A:ASN31 3.9 10.0 1.0 OD2 A:ASP32 4.0 27.7 1.0 O A:HOH830 4.0 35.4 1.0 CE A:LYS126 4.0 10.1 1.0 CA A:ASP32 4.0 15.0 1.0 OE1 A:GLN33 4.1 19.6 1.0 OD1 A:ASP32 4.1 26.8 1.0 CD A:GLN33 4.1 14.3 1.0 C A:ASN31 4.2 15.2 1.0 CA A:ASN31 4.3 15.6 1.0 O A:HOH774 4.3 14.2 1.0 ND2 A:ASN31 4.3 10.1 1.0 CG1 A:ILE130 4.3 13.3 1.0 O A:HOH831 4.3 23.3 1.0 OD1 A:ASN31 4.4 12.5 1.0 CD1 A:ILE130 4.4 10.0 1.0 O A:HOH771 4.4 21.8 1.0 N A:GLN33 4.7 13.9 1.0 O A:HOH769 4.8 72.3 1.0 C A:ASP32 4.9 14.9 1.0 CG A:LYS126 4.9 10.2 1.0

S.M.Wilbanks, D.B.Mckay. Structural Replacement of Active Site Monovalent Cations By the Epsilon-Amino Group of Lysine in the Atpase Fragment of Bovine HSC70. Biochemistry V. 37 7456 1998.
ISSN: ISSN 0006-2960
PubMed: 9585559
DOI: 10.1021/BI973046M