Zinc in PDB 5xky: Crystal Structure of Dddy Se Derivative

Protein crystallography data

The structure of Crystal Structure of Dddy Se Derivative, PDB code: 5xky was solved by C.Y.Li, Y.Z.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.74 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 61.221, 72.375, 88.341, 90.00, 90.00, 90.00
R / Rfree (%) 14.3 / 20.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Dddy Se Derivative (pdb code 5xky). 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 Dddy Se Derivative, PDB code: 5xky:

Zinc binding site 1 out of 1 in 5xky

Go back to Zinc Binding Sites List in 5xky
Zinc binding site 1 out of 1 in the Crystal Structure of Dddy Se Derivative


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 Dddy Se Derivative within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn500

b:26.4
occ:1.00
OE1 A:GLU269 2.1 16.8 1.0
NE2 A:HIS265 2.2 12.3 1.0
NE2 A:HIS338 2.3 17.1 1.0
O A:HOH867 2.4 23.5 1.0
O A:HOH608 2.6 18.8 1.0
CD A:GLU269 3.0 14.9 1.0
CD2 A:HIS338 3.1 12.5 1.0
CE1 A:HIS265 3.2 12.1 1.0
CD2 A:HIS265 3.2 11.3 1.0
OE2 A:GLU269 3.2 15.8 1.0
CE1 A:HIS338 3.4 12.2 1.0
NE2 A:HIS263 3.5 15.3 1.0
CD2 A:HIS263 3.7 14.8 1.0
ND1 A:HIS265 4.3 15.0 1.0
CG A:HIS265 4.3 14.4 1.0
CG A:GLU269 4.3 16.3 1.0
CG A:HIS338 4.3 15.2 1.0
NH2 A:ARG361 4.4 15.0 1.0
ND1 A:HIS338 4.4 13.6 1.0
OH A:TYR271 4.5 19.6 1.0
CE2 A:TYR271 4.6 12.0 1.0
CB A:GLU269 4.7 14.3 1.0
CE1 A:HIS263 4.7 12.5 1.0
CG A:HIS263 4.9 12.7 1.0

Reference:

C.Y.Li, D.Zhang, X.L.Chen, P.Wang, W.L.Shi, P.Y.Li, X.Y.Zhang, Q.L.Qin, J.D.Todd, Y.Z.Zhang. Mechanistic Insights Into Dimethylsulfoniopropionate Lyase Dddy, A New Member of the Cupin Superfamily. J. Mol. Biol. V. 429 3850 2017.
ISSN: ESSN 1089-8638
PubMed: 29106934
DOI: 10.1016/J.JMB.2017.10.022
Page generated: Wed Dec 16 11:20:41 2020

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