Chlorine in PDB 1jc7: The Laminin-Binding Domain of Agrin Is Structurally Related to N-Timp-1

The structure of The Laminin-Binding Domain of Agrin Is Structurally Related to N-Timp-1, PDB code: 1jc7 was solved by J.Stetefeld, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.92 / 2.73
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	85.306, 49.899, 54.328, 90.00, 118.43, 90.00
R / Rfree (%)	20.7 / 24.9

The binding sites of Chlorine atom in the The Laminin-Binding Domain of Agrin Is Structurally Related to N-Timp-1 (pdb code 1jc7). 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 The Laminin-Binding Domain of Agrin Is Structurally Related to N-Timp-1, PDB code: 1jc7:

Chlorine binding site 1 out of 1 in the The Laminin-Binding Domain of Agrin Is Structurally Related to N-Timp-1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Laminin-Binding Domain of Agrin Is Structurally Related to N-Timp-1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:15.3 occ:1.00 NH2 A:ARG5 3.2 38.7 1.0 OG A:SER108 3.2 27.3 1.0 CB A:GLU4 3.7 54.9 1.0 N A:SER108 3.9 27.7 1.0 N A:ARG5 4.0 34.6 1.0 CD A:ARG5 4.0 40.8 1.0 CA A:GLU4 4.0 41.8 1.0 CB A:SER107 4.1 27.3 1.0 CZ A:ARG5 4.1 37.4 1.0 CB A:SER108 4.4 23.5 1.0 CA A:SER107 4.4 24.9 1.0 NE A:ARG5 4.4 38.9 1.0 C A:GLU4 4.5 40.3 1.0 N A:CYS74 4.7 29.5 1.0 NE A:ARG10 4.7 37.0 1.0 C A:SER107 4.7 24.5 1.0 CA A:SER108 4.7 27.3 1.0 CA A:ILE73 4.8 25.8 1.0 CD A:ARG10 4.8 32.9 1.0 O A:LEU72 4.8 28.4 1.0 CG A:GLU4 4.9 56.5 1.0 CB A:ARG5 5.0 43.3 1.0 CG2 A:ILE73 5.0 21.6 1.0

J.Stetefeld, M.Jenny, T.Schulthess, R.Landwehr, B.Schumacher, S.Frank, M.A.Ruegg, J.Engel, R.A.Kammerer. The Laminin-Binding Domain of Agrin Is Structurally Related to N-Timp-1. Nat.Struct.Biol. V. 8 705 2001.
ISSN: ISSN 1072-8368
PubMed: 11473262
DOI: 10.1038/90422