Zinc in PDB 8r71: Polysaccharide Lyase BTPL33HA (BT4410) Y291A with HADP4 Collected at 1.22 A

The structure of Polysaccharide Lyase BTPL33HA (BT4410) Y291A with HADP4 Collected at 1.22 A, PDB code: 8r71 was solved by A.Cartmell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	60.66 / 1.92
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.633, 137.347, 202.832, 90, 90, 90
R / Rfree (%)	17.9 / 20.8

The binding sites of Zinc atom in the Polysaccharide Lyase BTPL33HA (BT4410) Y291A with HADP4 Collected at 1.22 A (pdb code 8r71). 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) Y291A with HADP4 Collected at 1.22 A, PDB code: 8r71:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Polysaccharide Lyase BTPL33HA (BT4410) Y291A with HADP4 Collected at 1.22 A


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) Y291A with HADP4 Collected at 1.22 A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn702 b:29.1 occ:1.00 HE2 A:HIS482 1.3 30.0 0.0 HD1 A:HIS438 1.4 30.0 0.0 O A:HOH856 2.1 25.6 1.0 NE2 A:HIS482 2.1 27.4 1.0 OD1 A:ASP456 2.2 25.1 1.0 O A:HOH860 2.2 25.1 1.0 ND1 A:HIS438 2.2 29.5 1.0 O A:HOH1024 2.3 24.5 1.0 CG A:ASP456 3.1 28.9 1.0 CE1 A:HIS482 3.1 27.7 1.0 CE1 A:HIS438 3.1 32.1 1.0 CD2 A:HIS482 3.1 27.4 1.0 HE1 A:HIS438 3.1 30.4 1.0 HD2 A:HIS482 3.2 27.4 1.0 HE1 A:HIS482 3.3 27.9 1.0 CG A:HIS438 3.3 33.1 1.0 OD2 A:ASP456 3.3 26.8 1.0 HB3 A:HIS438 3.6 34.3 1.0 H A:GLY458 3.6 24.2 1.0 HB2 A:HIS438 3.7 33.7 1.0 H A:ALA335 3.7 29.3 1.0 O A:HOH969 3.7 27.1 1.0 CB A:HIS438 3.8 35.1 1.0 O A:THR476 4.1 33.4 1.0 O A:ALA335 4.1 28.8 1.0 ND1 A:HIS482 4.1 28.3 1.0 CG A:HIS482 4.2 29.0 1.0 HA A:PHE334 4.2 28.2 1.0 NE2 A:HIS438 4.2 28.6 1.0 N A:ALA335 4.3 29.6 1.0 HA2 A:GLY458 4.3 23.4 1.0 H A:ALA457 4.3 24.6 1.0 CD2 A:HIS438 4.4 31.2 1.0 O A:ASN333 4.4 24.7 1.0 HB3 A:ASP440 4.4 30.5 1.0 N A:GLY458 4.4 24.5 1.0 CB A:ASP456 4.4 24.1 1.0 OD2 A:ASP440 4.5 29.5 1.0 HA A:ALA335 4.6 30.7 1.0 HA A:ASP456 4.7 24.8 1.0 C A:ALA335 4.7 28.7 1.0 N A:ALA457 4.7 24.4 1.0 HB3 A:ASP456 4.7 25.0 1.0 CA A:ALA335 4.8 31.1 1.0 CA A:GLY458 4.9 22.9 1.0 C A:ASP456 4.9 22.8 1.0 CA A:ASP456 4.9 25.8 1.0 HD1 A:HIS482 5.0 30.0 0.0 C A:PHE334 5.0 25.6 1.0

Zinc binding site 2 out of 2 in the Polysaccharide Lyase BTPL33HA (BT4410) Y291A with HADP4 Collected at 1.22 A


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) Y291A with HADP4 Collected at 1.22 A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn702 b:34.6 occ:1.00 HE2 B:HIS482 1.3 30.0 0.0 HD1 B:HIS438 1.4 30.0 0.0 O B:HOH814 1.8 27.2 1.0 NE2 B:HIS482 2.0 29.3 1.0 OD1 B:ASP456 2.1 33.2 1.0 O B:HOH849 2.2 28.1 1.0 ND1 B:HIS438 2.2 38.1 1.0 O B:HOH915 2.3 36.5 1.0 CD2 B:HIS482 2.9 28.7 1.0 CG B:ASP456 3.0 32.8 1.0 HD2 B:HIS482 3.1 29.1 1.0 CE1 B:HIS438 3.1 43.0 1.0 CE1 B:HIS482 3.1 31.0 1.0 HE1 B:HIS438 3.2 40.9 1.0 CG B:HIS438 3.3 41.1 1.0 OD2 B:ASP456 3.3 29.2 1.0 HE1 B:HIS482 3.4 30.9 1.0 HB3 B:HIS438 3.5 39.1 1.0 HB2 B:HIS438 3.7 38.8 1.0 H B:GLY458 3.7 34.1 1.0 H B:ALA335 3.7 33.9 1.0 CB B:HIS438 3.8 39.0 1.0 O B:HOH838 3.8 31.9 1.0 O B:THR476 4.0 38.8 1.0 CG B:HIS482 4.1 31.3 1.0 O B:ALA335 4.1 37.7 1.0 ND1 B:HIS482 4.2 30.9 1.0 N B:ALA335 4.3 33.2 1.0 NE2 B:HIS438 4.3 39.5 1.0 HA B:PHE334 4.3 33.9 1.0 H B:ALA457 4.3 32.6 1.0 HB3 B:ASP440 4.4 29.3 1.0 CB B:ASP456 4.4 29.1 1.0 CD2 B:HIS438 4.4 41.5 1.0 HA2 B:GLY458 4.4 36.1 1.0 OD2 B:ASP440 4.4 28.8 1.0 O B:ASN333 4.5 36.8 1.0 N B:GLY458 4.5 34.5 1.0 HA B:ALA335 4.5 36.3 1.0 HA B:ASP456 4.7 30.3 1.0 HB3 B:ASP456 4.7 30.2 1.0 N B:ALA457 4.7 33.1 1.0 C B:ALA335 4.8 40.9 1.0 CA B:ALA335 4.8 35.3 1.0 CA B:ASP456 4.9 30.6 1.0 C B:ASP456 4.9 31.2 1.0 O B:HOH980 4.9 30.0 1.0 HB2 B:ASP440 4.9 29.1 1.0 CA B:GLY458 5.0 35.5 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.