PDBsum entry 1apt

Hydrolase/hydrolase inhibitor

PDB id: 1apt

Contents

Protein chain

323 a.a. *

Ligands

IVA-VAL-VAL-LTA

MAN

Waters ×247

* Residue conservation analysis

PDB id:

1apt

Name:

Hydrolase/hydrolase inhibitor

Title:

Crystallographic analysis of a pepstatin analogue binding to the aspartyl proteinase penicillopepsin at 1.8 angstroms resolution

Structure:

Penicillopepsin. Chain: e. Engineered: yes. Inhibitor isovaleryl (iva)-val-val-lysta-o-et (lysta is a lysyl side chain analogue of statin. Chain: i. Engineered: yes. Other_details: transition state mimic inhibitor

Source:

Penicillium janthinellum. Penicillium vitale. Organism_taxid: 5079.

Biol. unit:

Tetramer (from PQS)

Resolution:

1.80Å R-factor: 0.135

Authors:

A.R.Sielecki,M.N.G.James

Key ref:

M.N.G.James et al. (1983). Crystallographic analysis of a pepstatin analogue binding to the aspartyl proteinase penicillopepsin at 1.8 angstroms resolution. Peptides: structure and, 1, 521.

Date:

16-Dec-91 Release date: 31-Jan-94

Protein chain

P00798  (PEPA1_PENJA) -  Penicillopepsin-1 from Penicillium janthinellum

Seq: 323 a.a.

Struc: 323 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.23.20 - penicillopepsin.
• Reaction: Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and activates trypsinogen.