Brand  (β version)

PDB ID: 1BTW

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Ligands
Code Name Style Show Link
0ZW N-(tert-butoxycarbonyl)-L-alanyl-N-{(1s)-5-ammonio-1-[hydroxy(3-hydroxypropoxy)boranyl]pentyl}-L-valinamide PoSSuM
CA Calcium ion PoSSuM
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Structure summary

Code : 1BTW   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Episelection: novel KI ~nanomolar inhibitors of serine proteases selected by binding or chemistry on an enzyme surface
Release Data : 1995-10-15
Compound :
mol_id molecule chains
1 BETA-TRYPSIN A
ec: 3.4.21.4
Source :
mol_id organism_scientific organism_common
1 Bos taurus  (taxid:9913) Cattle
Authors : Stroud, R.M., Katz, B.A., Finer-Moore, J.
Keywords : TRIPEPTIDEBORONATE 1, 3-PROPANEDIOL MONOESTER-INHIBITED, SERINE PROTEINASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
Exp. method : X-RAY DIFFRACTION ( 1.7 Å )
Citation :

Episelection: novel Ki approximately nanomolar inhibitors of serine proteases selected by binding or chemistry on an enzyme surface.

Katz, B.A.,Finer-Moore, J.,Mortezaei, R.  et al.
(1995)  Biochemistry  34 : 8264 - 8280

PubMed: 7599119
DOI: 10.1021/bi00026a008

Solvent Structure in Crystals of Trypsin Determined by X-Ray and Neutron Diffraction

Finer-Moore, J.S.,Kossiakoff, A.,Hurley, J.H.  et al.
(1992)  Proteins  12 : 203

1.59 Angstrom Structure of Trypsin at 120K: Comparison of Low Temperature and Room Temperature Structures

Earnest, T.,Fauman, E.,Craik, C.S.  et al.
(1991)  Proteins  10 : 171

Difference Fourier Refinement of the Structure of Dip-Trypsin at 1.5 Angstroms Using a Minicomputer Technique

Chambers, J.L.,Stroud, R.M.
(1977)  Acta Crystallogr.,Sect.B  33 : 1824

Structure and Specific Binding of Trypsin, Comparison of Inhibited Derivatives and a Model for Substrate Binding

Krieger, M.,Kay, L.M.,Stroud, R.M.
(1974)  J.Mol.Biol.  83 : 209

The Crystal and Molecular Structure of Dip-Inhibited Bovine Trypsin at 2.7 Angstroms Resolution

Stroud, R.M.,Kay, L.M.,Dickerson, R.E.
(1972)  Cold Spring Harbor Symp.Quant.Biol.  36 : 125

Reaction

Chain : A
UniProt : P00760 (TRY1_BOVIN)
Reaction: EC: Evidence:
Physiological Direction:
Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa. 3.4.21.4 -
-