Chlorine in PDB 6ggy: Paenibacillus Sp. YM1 Laminaribiose Phosphorylase with Sulphate Bound

All present enzymatic activity of Paenibacillus Sp. YM1 Laminaribiose Phosphorylase with Sulphate Bound:
2.4.1.31;

The structure of Paenibacillus Sp. YM1 Laminaribiose Phosphorylase with Sulphate Bound, PDB code: 6ggy was solved by S.Kuhaudomlarp, S.Walpole, C.E.M.Stevenson, S.A.Nepogodiev, D.M.Lawson, J.Angulo, R.A.Field, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	103.74 / 1.95
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	146.704, 146.704, 222.950, 90.00, 90.00, 90.00
R / Rfree (%)	20.2 / 22.3

The binding sites of Chlorine atom in the Paenibacillus Sp. YM1 Laminaribiose Phosphorylase with Sulphate Bound (pdb code 6ggy). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Paenibacillus Sp. YM1 Laminaribiose Phosphorylase with Sulphate Bound, PDB code: 6ggy:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Paenibacillus Sp. YM1 Laminaribiose Phosphorylase with Sulphate Bound


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Paenibacillus Sp. YM1 Laminaribiose Phosphorylase with Sulphate Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1007 b:53.7 occ:1.00 O A:HOH1310 3.3 44.2 1.0 N A:GLY370 3.4 52.0 1.0 N A:ARG368 3.6 47.0 1.0 CA A:GLY370 3.8 53.2 1.0 N A:GLY369 3.9 49.1 1.0 C A:ARG368 4.0 49.3 1.0 CB A:ARG368 4.0 49.6 1.0 CA A:ARG368 4.0 48.4 1.0 C A:GLY370 4.4 52.8 1.0 C A:GLY369 4.5 51.4 1.0 O A:ARG368 4.5 50.5 1.0 O A:GLY370 4.6 52.1 1.0 C A:GLY367 4.7 45.3 1.0 CA A:GLY369 4.8 50.0 1.0 CG A:ARG368 4.8 49.5 1.0 CA A:GLY367 4.9 44.3 1.0

Chlorine binding site 2 out of 4 in the Paenibacillus Sp. YM1 Laminaribiose Phosphorylase with Sulphate Bound


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Paenibacillus Sp. YM1 Laminaribiose Phosphorylase with Sulphate Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1008 b:65.7 occ:1.00 NH2 A:ARG92 3.2 39.0 1.0 NE A:ARG92 3.4 35.7 1.0 CZ A:ARG92 3.8 37.6 1.0 CG A:ARG92 4.5 32.0 1.0 CD A:ARG92 4.5 33.8 1.0

Chlorine binding site 3 out of 4 in the Paenibacillus Sp. YM1 Laminaribiose Phosphorylase with Sulphate Bound


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Paenibacillus Sp. YM1 Laminaribiose Phosphorylase with Sulphate Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1009 b:54.3 occ:1.00 N B:ARG368 3.3 22.4 1.0 O B:HOH1428 3.3 32.2 1.0 N B:GLY370 3.5 26.0 1.0 N B:GLY369 3.7 23.3 1.0 CA B:ARG368 3.8 23.5 1.0 C B:ARG368 3.8 23.5 1.0 CB B:ARG368 3.9 24.7 1.0 CA B:GLY370 4.0 27.1 1.0 C B:GLY367 4.3 21.0 1.0 CA B:GLY367 4.5 20.9 1.0 C B:GLY369 4.5 24.9 1.0 O B:ARG368 4.5 23.8 1.0 C B:GLY370 4.6 27.1 1.0 CG B:ARG368 4.6 25.9 1.0 O B:GLY370 4.6 27.6 1.0 CA B:GLY369 4.7 23.6 1.0 OG B:SER359 4.9 19.8 1.0

Chlorine binding site 4 out of 4 in the Paenibacillus Sp. YM1 Laminaribiose Phosphorylase with Sulphate Bound


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Paenibacillus Sp. YM1 Laminaribiose Phosphorylase with Sulphate Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1010 b:65.2 occ:1.00 NH2 B:ARG92 3.5 36.5 1.0 NE B:ARG92 3.6 33.4 1.0 O B:HOH1319 3.6 42.9 1.0 CE B:LYS122 3.7 44.7 1.0 NZ B:LYS122 4.0 47.1 1.0 CZ B:ARG92 4.0 34.5 1.0 CG B:ARG92 4.7 30.3 1.0 CD B:LYS122 4.7 43.4 1.0 CD B:ARG92 4.8 31.0 1.0

S.Kuhaudomlarp, S.Walpole, C.E.M.Stevenson, S.A.Nepogodiev, D.M.Lawson, J.Angulo, R.A.Field. Unravelling the Specificity of Laminaribiose Phosphorylase From Paenibacillus Sp. Ym-1 Towards Donor Substrates Glucose/Mannose 1-Phosphate By Using X-Ray Crystallography and Saturation Transfer Difference uc(Nmr) Spectroscopy. Chembiochem V. 20 181 2019.
ISSN: ESSN 1439-7633
PubMed: 29856496
DOI: 10.1002/CBIC.201800260