Zinc in PDB 5u2o: Crystal Structure of Zn-Binding Triple Mutant of Gh Family 9 Endoglucanase J30

The structure of Crystal Structure of Zn-Binding Triple Mutant of Gh Family 9 Endoglucanase J30, PDB code: 5u2o was solved by T.L.Ellinghaus, J.H.Pereira, R.P.Mcandrew, D.H.Welner, P.D.Adams, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	70.51 / 1.46
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	90.960, 90.960, 316.320, 90.00, 90.00, 120.00
R / Rfree (%)	14 / 15.1

The binding sites of Zinc atom in the Crystal Structure of Zn-Binding Triple Mutant of Gh Family 9 Endoglucanase J30 (pdb code 5u2o). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Zn-Binding Triple Mutant of Gh Family 9 Endoglucanase J30, PDB code: 5u2o:

Zinc binding site 1 out of 1 in the Crystal Structure of Zn-Binding Triple Mutant of Gh Family 9 Endoglucanase J30


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Zn-Binding Triple Mutant of Gh Family 9 Endoglucanase J30 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn606 b:11.2 occ:0.95 ND1 A:HIS115 2.1 10.6 1.0 NE2 A:HIS143 2.1 9.5 1.0 SG A:CYS98 2.3 10.9 1.0 SG A:CYS114 2.4 11.5 1.0 HA A:CYS98 2.8 11.4 1.0 HB2 A:HIS115 2.9 14.9 1.0 CE1 A:HIS143 3.0 9.4 1.0 CE1 A:HIS115 3.0 11.1 1.0 HB2 A:CYS114 3.1 13.2 1.0 CG A:HIS115 3.1 10.9 1.0 CD2 A:HIS143 3.1 9.3 1.0 HE1 A:HIS143 3.1 11.3 1.0 HE1 A:HIS115 3.2 13.3 1.0 CB A:CYS98 3.2 10.1 1.0 HB2 A:CYS98 3.3 12.2 1.0 H A:GLY99 3.3 12.2 1.0 CB A:CYS114 3.3 11.0 1.0 HD2 A:HIS143 3.3 11.1 1.0 CA A:CYS98 3.4 9.5 1.0 CB A:HIS115 3.5 12.4 1.0 HB2 A:PRO232 3.5 16.1 1.0 C A:CYS114 3.8 11.5 1.0 O A:CYS114 3.9 12.1 1.0 N A:GLY99 3.9 10.2 1.0 HB3 A:CYS114 4.1 13.2 1.0 HB3 A:CYS98 4.1 12.2 1.0 HB3 A:TYR148 4.1 12.4 1.0 NE2 A:HIS115 4.1 11.1 1.0 ND1 A:HIS143 4.1 10.1 1.0 HB3 A:HIS115 4.2 14.9 1.0 C A:CYS98 4.2 9.8 1.0 N A:HIS115 4.2 11.6 1.0 CA A:CYS114 4.2 11.7 1.0 CD2 A:HIS115 4.2 11.9 1.0 CG A:HIS143 4.2 9.0 1.0 HB3 A:PRO232 4.3 16.1 1.0 CB A:PRO232 4.3 13.4 1.0 CA A:HIS115 4.5 11.9 1.0 H A:HIS115 4.6 13.9 1.0 N A:CYS98 4.6 9.2 1.0 HH22 A:ARG239 4.7 15.3 1.0 H A:CYS114 4.8 14.7 1.0 O A:ARG97 4.8 9.7 1.0 HA A:CYS114 4.9 14.1 1.0 HE2 A:HIS115 4.9 13.3 1.0 HD1 A:HIS143 4.9 12.1 1.0 HD3 A:LYS150 4.9 11.8 1.0 NH2 A:ARG239 5.0 12.7 1.0

T.L.Ellinghaus, J.H.Pereira, R.P.Mcandrew, D.H.Welner, A.M.Degiovanni, J.M.Guenther, H.M.Tran, T.Feldman, B.A.Simmons, K.L.Sale, P.D.Adams. Engineering Glycoside Hydrolase Stability By the Introduction of Zinc Binding. Acta Crystallogr D Struct V. 74 702 2018BIOL.
ISSN: ISSN 2059-7983
PubMed: 29968680
DOI: 10.1107/S2059798318006678