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Zinc in PDB 5fsp: Structure of Thermolysin Prepared By the 'Soak-and-Freeze' Method Under 100 Bar of Krypton Pressure

Enzymatic activity of Structure of Thermolysin Prepared By the 'Soak-and-Freeze' Method Under 100 Bar of Krypton Pressure

All present enzymatic activity of Structure of Thermolysin Prepared By the 'Soak-and-Freeze' Method Under 100 Bar of Krypton Pressure:
3.4.24.27;

Protein crystallography data

The structure of Structure of Thermolysin Prepared By the 'Soak-and-Freeze' Method Under 100 Bar of Krypton Pressure, PDB code: 5fsp was solved by B.Lafumat, C.Mueller-Dieckmann, N.Colloc'h, T.Prange, A.Royant, P.Van Derlinden, P.Carpentier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.50 / 1.70
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.007, 93.007, 129.120, 90.00, 90.00, 120.00
R / Rfree (%) 15.5 / 17.8

Other elements in 5fsp:

The structure of Structure of Thermolysin Prepared By the 'Soak-and-Freeze' Method Under 100 Bar of Krypton Pressure also contains other interesting chemical elements:

Krypton (Kr) 8 atoms
Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Thermolysin Prepared By the 'Soak-and-Freeze' Method Under 100 Bar of Krypton Pressure (pdb code 5fsp). 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 Structure of Thermolysin Prepared By the 'Soak-and-Freeze' Method Under 100 Bar of Krypton Pressure, PDB code: 5fsp:

Zinc binding site 1 out of 1 in 5fsp

Go back to Zinc Binding Sites List in 5fsp
Zinc binding site 1 out of 1 in the Structure of Thermolysin Prepared By the 'Soak-and-Freeze' Method Under 100 Bar of Krypton Pressure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Thermolysin Prepared By the 'Soak-and-Freeze' Method Under 100 Bar of Krypton Pressure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1317

b:9.6
occ:1.00
 OE2 A:GLU166 2.0 11.5 1.0
NE2 A:HIS146 2.0 9.0 1.0
NE2 A:HIS142 2.0 10.0 1.0
O A:HOH2164 2.3 17.1 1.0
O A:HOH2165 2.5 36.9 1.0
CD A:GLU166 2.8 11.3 1.0
O A:HOH2166 2.8 37.6 1.0
CE1 A:HIS146 2.9 7.7 1.0
OE1 A:GLU166 3.0 11.7 1.0
CD2 A:HIS142 3.0 6.7 1.0
CE1 A:HIS142 3.0 10.3 1.0
CD2 A:HIS146 3.1 11.3 1.0
OH A:TYR157 4.0 15.2 1.0
ND1 A:HIS146 4.1 9.9 1.0
ND1 A:HIS142 4.1 8.3 1.0
CG A:HIS142 4.2 9.9 1.0
CG A:HIS146 4.2 7.9 1.0
NE2 A:HIS231 4.2 13.3 1.0
CG A:GLU166 4.2 10.0 1.0
O A:HOH2284 4.3 36.8 1.0
OE1 A:GLU143 4.4 12.2 1.0
CB A:SER169 4.4 10.1 1.0
N A:VAL2318 4.5 24.1 1.0
O A:HOH2148 4.6 15.7 1.0
OG A:SER169 4.6 9.8 1.0
O A:VAL2318 4.7 23.6 1.0
CD2 A:HIS231 4.8 13.8 1.0
CA A:GLU166 4.8 6.1 1.0
CZ A:TYR157 4.9 13.3 1.0
CA A:VAL2318 5.0 25.7 1.0
CE1 A:TYR157 5.0 11.9 1.0

Reference:

B.Lafumat, C.Mueller-Dieckmann, N.Colloc'h, T.Prange, A.Royant, P.Van Der Linden, P.Carpentier. Gas-Sensitive Biological Crystals Processed in Pressurized Oxygen and Krypton Atmospheres: Deciphering Gas Channels in Proteins Using A Novel `Soak-and-Freeze' Methodology. J.Appl.Crystallogr. V. 49 1478 2016.
ISSN: ISSN 0021-8898
DOI: 10.1107/S1600576716010992
Page generated: Sun Oct 27 16:30:08 2024

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