Zinc in PDB 8r6z: Polysaccharide Lyase BTPL33HA (BT4410) Apo Form 2

The structure of Polysaccharide Lyase BTPL33HA (BT4410) Apo Form 2, PDB code: 8r6z was solved by A.Cartmell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	113.85 / 2.03
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.529, 137.672, 202.506, 90, 90, 90
R / Rfree (%)	19.1 / 25.1

The binding sites of Zinc atom in the Polysaccharide Lyase BTPL33HA (BT4410) Apo Form 2 (pdb code 8r6z). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Polysaccharide Lyase BTPL33HA (BT4410) Apo Form 2, PDB code: 8r6z:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Polysaccharide Lyase BTPL33HA (BT4410) Apo Form 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Polysaccharide Lyase BTPL33HA (BT4410) Apo Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn701 b:26.2 occ:1.00 NE2 B:HIS490 2.1 17.6 1.0 OD1 B:ASP464 2.2 27.8 1.0 O B:HOH842 2.2 18.8 1.0 ND1 B:HIS446 2.2 24.2 1.0 O B:HOH852 2.3 20.8 1.0 O B:HOH907 2.4 20.3 1.0 CD2 B:HIS490 3.0 17.5 1.0 CE1 B:HIS446 3.0 26.0 1.0 CG B:ASP464 3.0 26.6 1.0 CE1 B:HIS490 3.2 17.2 1.0 OD2 B:ASP464 3.3 25.3 1.0 CG B:HIS446 3.3 23.8 1.0 CB B:HIS446 3.7 25.9 1.0 O B:HOH878 3.9 18.6 1.0 O B:THR484 4.0 31.7 1.0 O B:ALA343 4.1 20.8 1.0 CG B:HIS490 4.2 19.0 1.0 NE2 B:HIS446 4.2 25.8 1.0 ND1 B:HIS490 4.2 18.2 1.0 N B:ALA343 4.2 29.5 1.0 CD2 B:HIS446 4.3 22.0 1.0 N B:GLY466 4.4 22.6 1.0 CB B:ASP464 4.4 21.7 1.0 O B:ASN341 4.4 23.0 1.0 OD2 B:ASP448 4.5 21.2 1.0 N B:ALA465 4.7 21.6 1.0 C B:ALA343 4.7 23.0 1.0 CA B:ALA343 4.8 27.5 1.0 CA B:GLY466 4.8 21.5 1.0 CA B:ASP464 4.9 22.8 1.0 C B:ASP464 5.0 19.7 1.0

Zinc binding site 2 out of 2 in the Polysaccharide Lyase BTPL33HA (BT4410) Apo Form 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Polysaccharide Lyase BTPL33HA (BT4410) Apo Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:32.1 occ:1.00 O A:HOH817 1.8 19.1 1.0 NE2 A:HIS490 2.1 29.1 1.0 OD1 A:ASP464 2.1 32.9 1.0 O A:HOH836 2.2 18.4 1.0 ND1 A:HIS446 2.2 30.0 1.0 O A:HOH831 2.3 23.0 1.0 CD2 A:HIS490 3.0 29.6 1.0 CE1 A:HIS446 3.0 34.1 1.0 CG A:ASP464 3.0 31.3 1.0 CE1 A:HIS490 3.1 30.8 1.0 CG A:HIS446 3.3 32.1 1.0 OD2 A:ASP464 3.3 27.8 1.0 CB A:HIS446 3.7 30.5 1.0 O A:HOH819 3.8 23.2 1.0 O A:THR484 3.9 36.9 1.0 CG A:HIS490 4.2 28.1 1.0 O A:ALA343 4.2 40.1 1.0 ND1 A:HIS490 4.2 28.5 1.0 NE2 A:HIS446 4.2 37.2 1.0 N A:ALA343 4.2 33.2 1.0 CD2 A:HIS446 4.3 33.4 1.0 OD2 A:ASP448 4.4 27.8 1.0 CB A:ASP464 4.4 28.1 1.0 N A:GLY466 4.6 28.4 1.0 O A:ASN341 4.6 31.9 1.0 CA A:ALA343 4.7 40.2 1.0 N A:ALA465 4.7 33.3 1.0 C A:ALA343 4.8 42.0 1.0 C A:ASP464 4.9 31.6 1.0 CA A:ASP464 4.9 29.9 1.0

A.Cartmell, M.Couturier. Polysaccharide Lyase Family 33 Utilises An Evolutionary Conserved Mechanism of Conformationally Induced Catalysis to Drive Processivity To Be Published.