Zinc in PDB 1gw1: Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa

All present enzymatic activity of Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa:
3.2.1.78;

The structure of Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa, PDB code: 1gw1 was solved by V.Ducros, D.L.Zechel, H.J.Gilbert, L.Szabo, S.G.Withers, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.65
Space group	P 41
Cell size a, b, c (Å), α, β, γ (°)	93.488, 93.488, 53.719, 90.00, 90.00, 90.00
R / Rfree (%)	13.8 / 16.7

The structure of Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa also contains other interesting chemical elements:

Fluorine	(F)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Zinc atom in the Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa (pdb code 1gw1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa, PDB code: 1gw1:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1422 b:19.8 occ:1.00 N A:TRS1430 1.9 26.6 1.0 NE2 A:HIS71 2.0 15.9 1.0 OE2 A:GLU67 2.0 21.6 1.0 O2 A:TRS1430 2.5 21.7 1.0 C A:TRS1430 3.0 28.5 1.0 CD2 A:HIS71 3.0 16.3 1.0 CE1 A:HIS71 3.0 17.1 1.0 CD A:GLU67 3.0 24.3 1.0 C2 A:TRS1430 3.3 26.3 1.0 OE1 A:GLU67 3.4 24.9 1.0 C3 A:TRS1430 3.5 31.6 1.0 O3 A:TRS1430 3.6 33.1 1.0 ND1 A:HIS71 4.1 17.8 1.0 CG A:HIS71 4.1 16.0 1.0 O A:HOH2019 4.2 37.8 1.0 C1 A:TRS1430 4.3 31.7 1.0 O A:HOH2377 4.3 22.1 1.0 CG A:GLU67 4.3 24.8 1.0 O A:GLU67 4.5 24.2 1.0 O A:HOH2016 4.6 36.6 1.0

Zinc binding site 2 out of 2 in the Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1424 b:15.5 occ:0.50 NH1 A:ARG208 1.8 21.3 1.0 OD2 A:ASP283 1.9 23.1 1.0 OE1 A:GLU320 2.0 15.2 0.5 ND1 A:HIS211 2.1 16.8 0.5 OE1 A:GLU320 2.2 20.4 0.5 CD2 A:HIS211 2.4 14.3 0.5 CZ A:ARG208 2.8 19.1 1.0 CG A:ASP283 2.8 21.7 1.0 OD1 A:ASP283 2.9 25.9 1.0 NH2 A:ARG208 3.0 20.8 1.0 CD A:GLU320 3.0 18.4 0.5 CG A:HIS211 3.0 16.1 0.5 CE1 A:HIS211 3.1 17.4 0.5 CG A:HIS211 3.1 14.2 0.5 CD A:GLU320 3.3 20.4 0.5 CB A:HIS211 3.4 14.2 1.0 NE2 A:HIS211 3.5 17.1 0.5 CG A:GLU320 3.7 21.0 0.5 OE2 A:GLU320 3.9 17.8 0.5 CG A:GLU320 4.0 22.1 0.5 O A:HOH2279 4.0 28.3 1.0 NE A:ARG208 4.0 18.0 1.0 F2 A:MAF1427 4.0 19.6 0.5 CB A:GLU320 4.1 19.7 1.0 NE2 A:HIS211 4.1 18.2 0.5 CD2 A:HIS211 4.1 19.1 0.5 CB A:ASP283 4.1 18.1 1.0 OG A:SER255 4.2 19.4 0.5 ND1 A:HIS211 4.2 15.2 0.5 OG A:SER255 4.2 16.5 0.5 CE1 A:HIS211 4.4 15.9 0.5 OE2 A:GLU320 4.5 19.6 0.5 CD A:ARG208 4.6 18.2 1.0 C1 A:MAF1427 4.6 18.1 0.5 CA A:HIS211 4.8 12.6 1.0 CB A:SER319 4.9 18.1 1.0 CB A:SER255 4.9 16.9 0.5 N A:ALA212 4.9 13.3 1.0 CB A:SER255 4.9 16.0 0.5 C2 A:MAF1427 4.9 17.3 0.5 F2 A:MBF1428 5.0 20.6 0.5

V.Ducros, D.L.Zechel, G.Murshudov, H.J.Gilbert, L.Szabo, D.Stoll, S.G.Withers, G.J.Davies. Substrate Distortion By A Beta-Mannanase: Snapshots of the Michaelis and Covalent-Intermediate Complexes Suggest A B2,5 Conformation For the Transition State Angew.Chem.Int.Ed.Engl. V. 41 2824 2002.
ISSN: ISSN 1433-7851
PubMed: 12203498
DOI: 10.1002/1521-3773(20020802)41:15<2824::AID-ANIE2824>3.0.CO;2