Atomistry » Zinc » PDB 6d1a-6dbv » 6d5p
Atomistry »
  Zinc »
    PDB 6d1a-6dbv »
      6d5p »

Zinc in PDB 6d5p: Hexagonal Thermolysin Cryocooled to 100 K with 20% Xylose As Cryoprotectant

Enzymatic activity of Hexagonal Thermolysin Cryocooled to 100 K with 20% Xylose As Cryoprotectant

All present enzymatic activity of Hexagonal Thermolysin Cryocooled to 100 K with 20% Xylose As Cryoprotectant:
3.4.24.27;

Protein crystallography data

The structure of Hexagonal Thermolysin Cryocooled to 100 K with 20% Xylose As Cryoprotectant, PDB code: 6d5p was solved by D.H.Juers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 13.75 / 3.00
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.307, 93.307, 129.125, 90.00, 90.00, 120.00
R / Rfree (%) 23.3 / 30.8

Other elements in 6d5p:

The structure of Hexagonal Thermolysin Cryocooled to 100 K with 20% Xylose As Cryoprotectant also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Hexagonal Thermolysin Cryocooled to 100 K with 20% Xylose As Cryoprotectant (pdb code 6d5p). 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 Hexagonal Thermolysin Cryocooled to 100 K with 20% Xylose As Cryoprotectant, PDB code: 6d5p:

Zinc binding site 1 out of 1 in 6d5p

Go back to Zinc Binding Sites List in 6d5p
Zinc binding site 1 out of 1 in the Hexagonal Thermolysin Cryocooled to 100 K with 20% Xylose As Cryoprotectant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Hexagonal Thermolysin Cryocooled to 100 K with 20% Xylose As Cryoprotectant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn403

b:33.8
occ:0.96
OE2 A:GLU166 1.8 18.3 1.0
NE2 A:HIS142 2.1 22.2 1.0
NE2 A:HIS146 2.3 15.9 1.0
O A:HOH526 2.3 8.2 1.0
CD A:GLU166 2.8 27.9 1.0
CE1 A:HIS142 3.1 21.9 1.0
CD2 A:HIS142 3.1 24.2 1.0
OE1 A:GLU166 3.1 29.3 1.0
CD2 A:HIS146 3.1 22.6 1.0
HD2 A:HIS146 3.2 27.2 1.0
HE1 A:HIS142 3.2 26.3 1.0
HD2 A:HIS142 3.3 29.1 1.0
CE1 A:HIS146 3.3 11.2 1.0
HH A:TYR157 3.3 8.6 0.6
HA A:VAL401 3.5 35.8 1.0
HE1 A:HIS146 3.5 13.5 1.0
OH A:TYR157 4.0 7.2 0.6
NE2 A:HIS231 4.0 48.0 1.0
CG A:GLU166 4.2 36.1 1.0
OE1 A:GLU143 4.2 9.2 1.0
HA A:GLU166 4.2 33.7 1.0
ND1 A:HIS142 4.2 15.1 1.0
HB2 A:SER169 4.2 15.5 1.0
HG2 A:GLU166 4.2 43.3 1.0
CG A:HIS142 4.2 19.5 1.0
HD2 A:HIS231 4.3 31.2 1.0
CA A:VAL401 4.3 29.9 1.0
CG A:HIS146 4.3 21.6 1.0
HB3 A:SER169 4.4 15.5 1.0
ND1 A:HIS146 4.4 22.6 1.0
HE2 A:TYR157 4.4 33.8 0.6
CD2 A:HIS231 4.5 26.0 1.0
O A:VAL401 4.6 25.4 1.0
C A:VAL401 4.6 29.6 1.0
CB A:SER169 4.6 12.9 1.0
N A:VAL401 4.7 24.2 1.0
HG3 A:GLU166 4.7 43.3 1.0
OE2 A:GLU143 4.8 13.3 1.0
CD A:GLU143 4.8 18.6 1.0
OG A:SER169 4.9 14.3 1.0
HH22 A:ARG203 4.9 23.6 1.0
CZ A:TYR157 4.9 11.3 0.6
HD1 A:HIS142 5.0 18.1 1.0

Reference:

D.H.Juers, C.A.Farley, C.P.Saxby, R.A.Cotter, J.K.B.Cahn, R.C.Holton-Burke, K.Harrison, Z.Wu. The Impact of Cryosolution Thermal Contraction on Proteins and Protein Crystals: Volumes, Conformation and Order. Acta Crystallogr D Struct V. 74 922 2018BIOL.
ISSN: ISSN 2059-7983
PubMed: 30198901
DOI: 10.1107/S2059798318008793
Page generated: Wed Dec 16 11:39:06 2020

Last articles

Zn in 7M6U
Zn in 7NNG
Zn in 7NEE
Zn in 7NEU
Zn in 7M3K
Zn in 7KWD
Zn in 7KYH
Zn in 7KNG
Zn in 7KY2
Zn in 7KYF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy