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Ligands
Code Name Style Show Link
ZN Zinc ion
CA Calcium ion
0PQ N-{(2r)-3-[(S)-[(1r)-1-amino-2-phenylethyl](hydroxy)phosphoryl]-2-benzylpropanoyl}-L-phenylalanine
DMS Dimethyl sulfoxide
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Code : 1OS0   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Thermolysin with an alpha-amino phosphinic inhibitor
Release Data : 2003-03-25
Compound :
mol_id molecule chains synonym
1 Thermolysin A Thermostable neutral proteinase
ec: 3.4.24.27
Source :
mol_id organism_scientific
1 Bacillus thermoproteolyticus  (taxid:1427)
Authors : Selkti, M., Tomas, A., Prange, T.
Keywords : THERMOLYSIN, ALPHA-AMINO PHOSPHINIC COMPOUND, NEPRYLISIN, HYDROLASE, Metal-binding, Metalloprotease, Protease, Secreted, Zymogen, HYDROLASE-HYDROLASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 2.10 Å )
Citation :

Interactions of a new alpha-aminophosphinic derivative inside the active site of TLN (thermolysin): a model for zinc-metalloendopeptidase inhibition.

Selkti, M.,Tomas, A.,Gaucher, J.F.  et al.
(2003)  Acta Crystallogr.,Sect.D  59 : 1200 - 1205

PubMed: 12832763
DOI: 10.1107/S0907444903010060

Crystal structures of alpha-mercaptoacyldipeptides in the Thermolysin active site: Structural parameters for a Zn Monodentation or bidentation in metalloendopeptidases

Gaucher, J.F.,Selkti, M.,Tiraboschi, G.  et al.
(1999)  Biochemistry  38 : 12569 - 12576

DOI: 10.1021/bi991043z

Chain : A
UniProt : P00800 (THER_BACTH)
Reaction: EC: Evidence:
Physiological Direction:
Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe. 3.4.24.27 -
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