Atomistry » Zinc » PDB 1q63-1qlj » 1qf1
Atomistry »
  Zinc »
    PDB 1q63-1qlj »
      1qf1 »

Zinc in PDB 1qf1: Thermolysin (E.C.3.4.24.27) Complexed with (2-Sulphanylheptanoyl)-Phe- Ala. Parameters For Zn-Bidentation of Mercaptoacyldipeptides in Metalloendopeptidase

Enzymatic activity of Thermolysin (E.C.3.4.24.27) Complexed with (2-Sulphanylheptanoyl)-Phe- Ala. Parameters For Zn-Bidentation of Mercaptoacyldipeptides in Metalloendopeptidase

All present enzymatic activity of Thermolysin (E.C.3.4.24.27) Complexed with (2-Sulphanylheptanoyl)-Phe- Ala. Parameters For Zn-Bidentation of Mercaptoacyldipeptides in Metalloendopeptidase:
3.4.24.27;

Protein crystallography data

The structure of Thermolysin (E.C.3.4.24.27) Complexed with (2-Sulphanylheptanoyl)-Phe- Ala. Parameters For Zn-Bidentation of Mercaptoacyldipeptides in Metalloendopeptidase, PDB code: 1qf1 was solved by J.-F.Gaucher, M.Selkti, G.Tiraboschi, T.Prange, B.P.Roques, A.Tomas, M.C.Fournie-Zaluski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.00
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.310, 93.310, 131.820, 90.00, 90.00, 120.00
R / Rfree (%) 16.5 / 22.4

Other elements in 1qf1:

The structure of Thermolysin (E.C.3.4.24.27) Complexed with (2-Sulphanylheptanoyl)-Phe- Ala. Parameters For Zn-Bidentation of Mercaptoacyldipeptides in Metalloendopeptidase also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Thermolysin (E.C.3.4.24.27) Complexed with (2-Sulphanylheptanoyl)-Phe- Ala. Parameters For Zn-Bidentation of Mercaptoacyldipeptides in Metalloendopeptidase (pdb code 1qf1). 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 (E.C.3.4.24.27) Complexed with (2-Sulphanylheptanoyl)-Phe- Ala. Parameters For Zn-Bidentation of Mercaptoacyldipeptides in Metalloendopeptidase, PDB code: 1qf1:

Zinc binding site 1 out of 1 in 1qf1

Go back to Zinc Binding Sites List in 1qf1
Zinc binding site 1 out of 1 in the Thermolysin (E.C.3.4.24.27) Complexed with (2-Sulphanylheptanoyl)-Phe- Ala. Parameters For Zn-Bidentation of Mercaptoacyldipeptides in Metalloendopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Thermolysin (E.C.3.4.24.27) Complexed with (2-Sulphanylheptanoyl)-Phe- Ala. Parameters For Zn-Bidentation of Mercaptoacyldipeptides in Metalloendopeptidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn320

b:6.8
occ:1.00
 OE2 A:GLU166 2.0 8.4 1.0
NE2 A:HIS142 2.1 9.4 1.0
NE2 A:HIS146 2.2 8.6 1.0
SG A:TI1317 2.3 8.4 1.0
O1 A:TI1317 2.4 7.5 1.0
CD A:GLU166 2.9 6.7 1.0
C1 A:TI1317 3.0 9.2 1.0
CD2 A:HIS146 3.0 5.6 1.0
CE1 A:HIS142 3.1 9.0 1.0
CD2 A:HIS142 3.1 6.8 1.0
OE1 A:GLU166 3.2 6.3 1.0
CE1 A:HIS146 3.2 5.0 1.0
CA1 A:TI1317 3.3 8.8 1.0
OH A:TYR157 3.9 6.5 1.0
CB1 A:TI1317 3.9 12.7 1.0
N2 A:TI1317 4.0 6.7 1.0
CG A:HIS146 4.2 5.3 1.0
ND1 A:HIS142 4.2 7.6 1.0
CG A:HIS142 4.3 8.4 1.0
ND1 A:HIS146 4.3 6.4 1.0
NE2 A:HIS231 4.3 7.5 1.0
OE1 A:GLU143 4.3 5.7 1.0
CG A:GLU166 4.3 5.0 1.0
CA2 A:TI1317 4.5 8.2 1.0
O A:DMS325 4.7 51.6 1.0
CB A:SER169 4.8 5.0 1.0
OE2 A:GLU143 4.8 7.5 1.0
CZ A:TYR157 4.8 6.8 1.0
OG A:SER169 4.9 5.3 1.0
CD A:GLU143 4.9 5.8 1.0
CE1 A:TYR157 4.9 7.6 1.0
CD2 A:HIS231 5.0 6.4 1.0

Reference:

J.F.Gaucher, M.Selkti, G.Tiraboschi, T.Prange, B.P.Roques, A.Tomas, M.C.Fournie-Zaluski. Crystal Structures of Alpha-Mercaptoacyldipeptides in the Thermolysin Active Site: Structural Parameters For A Zn Monodentation or Bidentation in Metalloendopeptidases. Biochemistry V. 38 12569 1999.
ISSN: ISSN 0006-2960
PubMed: 10504225
DOI: 10.1021/BI991043Z
Page generated: Wed Dec 16 03:01:46 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy