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Ligands
Code Name Style Show Link
0FG D-leucyl-N-(4-fluorobenzyl)-L-phenylalaninamide
SO4 Sulfate ion
Non-standard Residues
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Glycosylation
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Code : 1AFQ   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : CRYSTAL STRUCTURE OF BOVINE GAMMA-CHYMOTRYPSIN COMPLEXED WITH A SYNTHETIC INHIBITOR
Release Data : 1997-09-17
Compound :
mol_id molecule chains
1 BOVINE GAMMA-CHYMOTRYPSIN A
ec: 3.4.21.1
mol_id molecule chains
2 BOVINE GAMMA-CHYMOTRYPSIN B
ec: 3.4.21.1
mol_id molecule chains
3 BOVINE GAMMA-CHYMOTRYPSIN C
ec: 3.4.21.1
Source :
mol_id organism_scientific organism_common
1 Bos taurus  (taxid:9913) Cattle
organ: PANCREAS
mol_id organism_scientific organism_common
2 Bos taurus  (taxid:9913) Cattle
organ: PANCREAS
mol_id organism_scientific organism_common
3 Bos taurus  (taxid:9913) Cattle
organ: PANCREAS
Authors : Sugio, S., Kashima, A., Inoue, Y., Maeda, I., Nose, T., Shimohigashi, Y.
Keywords : HYDROLASE-HYDROLASE INHIBITOR COMPLEX
Exp. method : X-RAY DIFFRACTION ( 1.80 Å )
Citation :

X-ray crystal structure of a dipeptide-chymotrypsin complex in an inhibitory interaction.

Kashima, A.,Inoue, Y.,Sugio, S.  et al.
(1998)  Eur.J.Biochem.  255 : 12 - 23

PubMed: 9692896
DOI: 10.1046/j.1432-1327.1998.2550012.x

Gamma-Chymotrypsin is a Complex of Alpha-Chymotrypsin with its Own Autolysis Products

Harel, M.,Su, C.-T.,Frolow, F.  et al.
(1991)  Biochemistry  30 : 5217

Structure of Gamma-Chymotrypsin in the Range Ph 2.0 To Ph 10.5 Suggests that Gamma-Chymotrypsin is a Covalent Acyl-Enzyme Adduct at Low Ph

Dixon, M.M.,Brennan, R.G.,Matthews, B.W.
(1991)  Int.J.Biol.Macromol.  13 : 89

Is Gamma-Chymotrypsin a Tetrapeptide Acyl-Enzyme Adduct of Alpha-Chymotrypsin?

Dixon, M.M.,Matthews, B.W.
(1989)  Biochemistry  28 : 7033

Chain : C
UniProt : P00766 (CTRA_BOVIN)
Reaction: EC: Evidence:
Physiological Direction:
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|- Xaa. 3.4.21.1 PROSITE-ProRule:PRU10078, PROSITE-ProRule:PRU10079
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