Chlorine in PDB 5hpo: Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose

The structure of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose, PDB code: 5hpo was solved by A.S.Halavaty, S.H.Light, G.Minasov, J.Winsor, S.Grimshaw, L.Shuvalova, S.Peterson, W.F.Anderson, Center For Structural Genomics Of Infectiousdiseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.92 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	162.646, 100.131, 73.281, 90.00, 105.47, 90.00
R / Rfree (%)	13.3 / 16.4

The structure of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Calcium	(Ca)	1 atom

The binding sites of Chlorine atom in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose (pdb code 5hpo). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose, PDB code: 5hpo:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1104 b:33.3 occ:1.00 O A:HOH2179 3.1 47.7 1.0 NE A:ARG991 3.1 21.6 1.0 OG1 A:THR1025 3.3 29.1 1.0 O A:HOH2108 3.4 54.6 1.0 O A:HOH2278 3.4 38.2 1.0 CD A:ARG991 3.8 20.0 1.0 C A:ASN1024 3.8 21.0 1.0 CA A:ASN1024 3.9 21.0 1.0 O A:TRP1023 3.9 20.3 1.0 N A:THR1025 4.0 21.4 1.0 C A:TRP1023 4.0 20.4 1.0 N A:ASN1024 4.0 19.2 1.0 CZ A:ARG991 4.0 21.9 1.0 CG A:ARG991 4.1 18.4 1.0 NH2 A:ARG991 4.1 22.3 1.0 O A:ASN1024 4.2 19.2 1.0 CB A:TRP1023 4.2 20.1 1.0 CB A:THR1025 4.3 27.6 1.0 CA A:THR1025 4.7 23.2 1.0 CA A:TRP1023 4.8 20.8 1.0

Chlorine binding site 2 out of 2 in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Maltopentaose within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1105 b:48.1 occ:1.00 O A:HOH1861 3.2 39.8 1.0 N A:VAL124 3.2 26.4 1.0 OD2 A:ASP179 3.4 36.1 1.0 CA A:SER123 3.7 28.2 1.0 NZ A:LYS197 3.9 33.1 1.0 O A:VAL124 3.9 23.9 1.0 C A:SER123 3.9 27.3 1.0 CB A:VAL124 4.0 26.8 1.0 CA A:VAL124 4.1 24.9 1.0 CB A:SER123 4.1 29.7 1.0 CG2 A:VAL124 4.2 27.9 1.0 CG A:ASP179 4.3 34.2 1.0 OD1 A:ASP179 4.4 35.4 1.0 C A:VAL124 4.5 24.5 1.0 O A:THR122 4.8 29.3 1.0 N A:SER123 4.9 27.5 1.0

S.H.Light, L.A.Cahoon, K.V.Mahasenan, M.Lee, B.Boggess, A.S.Halavaty, S.Mobashery, N.E.Freitag, W.F.Anderson. Transferase Versus Hydrolase: the Role of Conformational Flexibility in Reaction Specificity. Structure V. 25 295 2017.
ISSN: ISSN 1878-4186
PubMed: 28089449
DOI: 10.1016/J.STR.2016.12.007