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Zinc in PDB 1tlx: Thermolysin (Native)

Enzymatic activity of Thermolysin (Native)

All present enzymatic activity of Thermolysin (Native):
3.4.24.27;

Protein crystallography data

The structure of Thermolysin (Native), PDB code: 1tlx was solved by A.C.English, S.H.Done, C.R.Groom, R.E.Hubbard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.10
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.910, 93.910, 131.170, 90.00, 90.00, 120.00
R / Rfree (%) 15.3 / 21.4

Other elements in 1tlx:

The structure of Thermolysin (Native) also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Thermolysin (Native) (pdb code 1tlx). 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 Thermolysin (Native), PDB code: 1tlx:

Zinc binding site 1 out of 1 in 1tlx

Go back to Zinc Binding Sites List in 1tlx
Zinc binding site 1 out of 1 in the Thermolysin (Native)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Thermolysin (Native) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:22.1
occ:1.00
NE2 A:HIS146 2.0 20.1 1.0
NE2 A:HIS142 2.0 17.3 1.0
O A:HOH1002 2.1 49.9 1.0
OE1 A:GLU166 2.2 24.9 1.0
OE2 A:GLU166 2.3 30.3 1.0
CD A:GLU166 2.8 23.3 1.0
O A:HOH1001 2.9 58.5 1.0
CE1 A:HIS146 2.9 17.1 1.0
CE1 A:HIS142 3.0 14.7 1.0
CD2 A:HIS146 3.0 16.2 1.0
CD2 A:HIS142 3.1 19.5 1.0
OH A:TYR157 3.7 22.2 0.4
OE2 A:GLU143 4.1 36.6 0.7
ND1 A:HIS146 4.1 18.6 1.0
ND1 A:HIS142 4.2 14.7 1.0
CG A:HIS146 4.2 17.9 1.0
CG A:HIS142 4.2 16.4 1.0
NE2 A:HIS231 4.3 25.5 1.0
CG A:GLU166 4.3 18.5 1.0
OE1 A:GLU143 4.4 24.5 0.7
CB A:SER169 4.4 16.0 1.0
OE1 A:GLU143 4.5 17.6 0.3
CA A:VAL317 4.5 33.4 1.0
O A:HOH1085 4.6 39.4 1.0
CD A:GLU143 4.6 27.0 0.7
CA A:GLU166 4.7 17.4 1.0
OG A:SER169 4.7 18.1 1.0
CZ A:TYR157 4.8 23.0 0.4
CD2 A:HIS231 4.8 30.7 1.0
CB A:GLU166 4.9 16.3 1.0
N A:VAL317 4.9 30.4 1.0
CE1 A:TYR157 4.9 25.0 0.4
C A:VAL317 5.0 32.6 1.0

Reference:

A.C.English, S.H.Done, L.S.Caves, C.R.Groom, R.E.Hubbard. Locating Interaction Sites on Proteins: the Crystal Structure of Thermolysin Soaked in 2% to 100% Isopropanol. Proteins V. 37 628 1999.
ISSN: ISSN 0887-3585
PubMed: 10651278
DOI: 10.1002/(SICI)1097-0134(19991201)37:4<628::AID-PROT13>3.3.CO;2-7
Page generated: Mon Jan 25 16:14:07 2021

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