Chlorine in PDB 5hxm: Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose

All present enzymatic activity of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose:
3.2.1.177;

The structure of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose, PDB code: 5hxm 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)	29.74 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	166.157, 102.437, 74.011, 90.00, 103.78, 90.00
R / Rfree (%)	15.2 / 19.5

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

Magnesium	(Mg)	5 atoms
Calcium	(Ca)	1 atom

The binding sites of Chlorine atom in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose (pdb code 5hxm). 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 Panose, PDB code: 5hxm:
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 Panose


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 Panose within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1107 b:56.1 occ:1.00 O A:HOH1961 3.0 64.5 1.0 NE A:ARG991 3.1 39.0 1.0 OG1 A:THR1025 3.2 51.7 1.0 CD A:ARG991 3.5 39.6 1.0 C A:ASN1024 3.5 45.0 1.0 N A:THR1025 3.6 46.7 1.0 CA A:ASN1024 3.7 44.9 1.0 O A:TRP1023 3.8 42.0 1.0 CB A:THR1025 3.9 49.9 1.0 N A:ASN1024 3.9 43.7 1.0 C A:TRP1023 3.9 44.1 1.0 CG A:ARG991 4.0 37.5 1.0 O A:ASN1024 4.1 44.7 1.0 CZ A:ARG991 4.1 39.9 1.0 CA A:THR1025 4.3 46.1 1.0 CB A:TRP1023 4.3 43.4 1.0 NH2 A:ARG991 4.4 40.5 1.0 CA A:TRP1023 4.8 43.6 1.0 CB A:ARG991 5.0 35.3 1.0

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


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 Panose within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1108 b:53.0 occ:1.00 O A:HOH1736 3.1 38.5 1.0 O A:HOH1997 3.1 44.9 1.0 N A:THR1031 3.4 42.4 1.0 CB A:ILE1005 3.6 33.2 1.0 CG1 A:ILE1005 3.6 33.6 1.0 CG2 A:ILE1005 3.9 33.8 1.0 CA A:VAL1030 3.9 42.2 1.0 CB A:THR1031 4.0 42.7 1.0 O A:HOH2118 4.1 49.2 1.0 O A:THR1031 4.1 41.6 1.0 C A:VAL1030 4.1 41.8 1.0 CA A:THR1031 4.2 41.2 1.0 NE2 A:GLN1010 4.2 35.8 1.0 CD A:LYS1008 4.2 33.4 1.0 OG1 A:THR1031 4.3 44.6 1.0 CB A:VAL1030 4.5 41.3 1.0 C A:THR1031 4.6 40.1 1.0 O A:PRO1029 4.7 40.6 1.0 CG A:LYS1008 4.8 32.2 1.0 CG1 A:VAL1030 4.8 41.9 1.0 CB A:LYS1008 4.8 31.8 1.0 CD1 A:ILE1005 4.8 33.4 1.0 CE A:LYS1008 4.9 36.0 1.0 NZ A:LYS1008 5.0 39.1 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