Chlorine in PDB 5y7c: Hapalindole A and Dmspp Bound AMBP3

The structure of Hapalindole A and Dmspp Bound AMBP3, PDB code: 5y7c was solved by C.P.Wong, T.Awakawa, Y.Nakashima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.84 / 2.00
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	46.465, 54.724, 77.991, 105.23, 106.60, 98.51
R / Rfree (%)	19.5 / 24.3

The binding sites of Chlorine atom in the Hapalindole A and Dmspp Bound AMBP3 (pdb code 5y7c). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Hapalindole A and Dmspp Bound AMBP3, PDB code: 5y7c:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Hapalindole A and Dmspp Bound AMBP3


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Hapalindole A and Dmspp Bound AMBP3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:51.7 occ:1.00 CL01 A:8O0402 0.0 51.7 1.0 C14 A:8O0402 1.8 44.9 1.0 C15 A:8O0402 2.7 41.6 1.0 C13 A:8O0402 2.8 39.3 1.0 C19 A:8O0402 3.2 38.1 1.0 C20 A:8O0402 3.2 32.2 1.0 C16 A:8O0402 3.3 34.0 1.0 CB A:ALA44 3.7 18.0 1.0 C14 A:DST401 3.8 40.5 1.0 CG1 A:VAL284 3.8 40.0 1.0 C10 A:8O0402 4.2 44.7 1.0 C12 A:8O0402 4.2 43.2 1.0 OD2 A:ASP277 4.2 39.8 1.0 NH1 A:ARG60 4.3 27.9 1.0 CG A:ARG60 4.4 21.4 1.0 CG2 A:VAL284 4.4 31.6 1.0 CB A:ASP277 4.7 21.7 1.0 C09 A:8O0402 4.7 41.5 1.0 CB A:VAL284 4.7 35.3 1.0 CG A:ASP277 4.8 30.7 1.0 N02 A:8O0402 4.8 40.9 1.0 C12 A:DST401 4.8 47.8 1.0 C11 A:DST401 4.9 41.3 1.0 CD A:ARG60 4.9 24.2 1.0

Chlorine binding site 2 out of 2 in the Hapalindole A and Dmspp Bound AMBP3


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Hapalindole A and Dmspp Bound AMBP3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl402 b:48.4 occ:1.00 CL01 B:8O0402 0.0 48.4 1.0 C14 B:8O0402 1.8 42.2 1.0 C15 B:8O0402 2.7 42.1 1.0 C13 B:8O0402 2.8 35.3 1.0 C19 B:8O0402 3.2 36.9 1.0 C16 B:8O0402 3.3 32.2 1.0 C20 B:8O0402 3.4 30.0 1.0 CB B:ALA44 3.6 18.9 1.0 CG1 B:VAL284 3.8 38.3 1.0 O B:HOH593 3.9 35.4 1.0 OD1 B:ASP277 3.9 40.6 1.0 C14 B:DST401 4.0 41.3 1.0 CD1 B:LEU259 4.1 35.0 1.0 C10 B:8O0402 4.2 41.6 1.0 C12 B:8O0402 4.2 40.6 1.0 NH1 B:ARG60 4.3 30.1 1.0 CG B:ARG60 4.3 23.3 1.0 CG2 B:VAL284 4.3 33.2 1.0 C12 B:DST401 4.4 47.5 1.0 CB B:ASP277 4.5 20.8 1.0 CG B:ASP277 4.6 34.0 1.0 CB B:VAL284 4.7 33.9 1.0 N02 B:8O0402 4.7 39.4 1.0 C09 B:8O0402 4.7 42.1 1.0 C13 B:DST401 4.8 42.2 1.0 CD B:ARG60 4.9 28.7 1.0 CA B:ALA44 5.0 22.1 1.0

C.P.Wong, T.Awakawa, Y.Nakashima, T.Mori, Q.Zhu, X.Liu, I.Abe. Two Distinct Substrate Binding Modes For the Normal and Reverse Prenylation of Hapalindoles By the Prenyltransferase AMBP3 Angew. Chem. Int. Ed. Engl. V. 57 560 2018.
ISSN: ESSN 1521-3773
PubMed: 29178634
DOI: 10.1002/ANIE.201710682