Brand  (β version)

PDB ID: 1P01

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Ligands
Code Name Style Show Link
0EG N-(tert-butoxycarbonyl)-L-alanyl-N-[(1r)-1-(dihydroxyboranyl)-2-methylpropyl]-L-prolinamide PoSSuM
SO4 Sulfate ion PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 1P01   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Serine protease mechanism. structure of an inhibitory complex oF ALPHA-LYTIC Protease and a tightly bound peptide boronic acid
Release Data : 1990-04-15
Compound :
mol_id molecule chains
1 ALPHA-LYTIC PROTEASE A
ec: 3.4.21.12
Source :
mol_id organism_scientific
1 Lysobacter enzymogenes  (taxid:69)
gene: alpha-LP
Authors : Bone, R., Agard, D.A.
Keywords : HYDROLASE-HYDROLASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 2.0 Å )
Citation :

Serine protease mechanism: structure of an inhibitory complex of alpha-lytic protease and a tightly bound peptide boronic acid.

Bone, R.,Shenvi, A.B.,Kettner, C.A.  et al.
(1987)  Biochemistry  26 : 7609 - 7614

PubMed: 3122831
DOI: 10.1021/bi00398a012

Structure Analysis of Specificity. Alpha-Lytic Protease Complexes with Analogs of Reaction Intermediates

Bone, R.,Frank, D.,Kettner, C.  et al.
To be Published 

Structural Plasticity as a Determinant of Enzyme Specificity. Creating Broadly Specific Proteases

Bone, R.,Silen, J.L.,Agard, D.A.
To be Published 

Kinetic Properties of the Binding of Alpha-Lytic Protease to Peptide Boronic Acids

Kettner, C.A.,Bone, R.,Agard, D.A.  et al.
(1988)  Biochemistry  27 : 7682

Refined Structure of Alpha-Lytic Protease at 1.7 Angstroms Resolution. Analysis of Hydrogen Bonding and Solvent Structure

Fujinaga, M.,Delbaere, L.T.J.,Brayer, G.D.  et al.
(1985)  J.Mol.Biol.  184 : 479

Molecular Structure of the Alpha-Lytic Protease from Myxobacter 495 at 2.8 Angstroms Resolution

Brayer, G.D.,Delbaere, L.T.J.,James, M.N.G.
(1979)  J.Mol.Biol.  131 : 743

Reaction

Chain : A
UniProt : P00778 (PRLA_LYSEN)
Reaction: EC: Evidence:
Physiological Direction:
Preferential cleavage: Ala-|-Xaa, Val-|-Xaa in bacterial cell walls, elastin and other proteins. 3.4.21.12 -
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