4ape

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THE ACTIVE SITE OF ASPARTIC PROTEINASES

Structural highlights

4ape is a 1 chain structure with sequence from Crypa. This structure supersedes the now removed PDB entries 2ape and 1ape. The December 2000 RCSB PDB Molecule of the Month feature on Pepsin by David S. Goodsell is 10.2210/rcsb_pdb/mom_2000_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:Endothiapepsin, with EC number 3.4.23.22
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The active site of the aspartic proteinase, endothiapepsin, has been defined by X-ray analysis and restrained least-squares refinement at 2.1 A resolution with a crystallographic agreement value of 0.16. The environments of the two catalytically important aspartyl groups are remarkably similar and the contributions of the NH2- and COOH-terminal domains to the catalytic centre are related by a local 2-fold axis. The carboxylates of the aspartyls share a hydrogen bond and have equivalent contacts to a bound water molecule or hydroxonium ion lying on the local diad. The main chains around 32 and 215 are connected by a novel interaction involving diad-related threonines. It is suggested that the two pKa values of the active site aspartyls arise from a structure not unlike that in maleic acid with a hydrogen-bonded intermediate species and a dicarboxylate characterised by electrostatic repulsions between the two negatively charged groups.

The active site of aspartic proteinases.,Pearl L, Blundell T FEBS Lett. 1984 Aug 20;174(1):96-101. PMID:6381096[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
15 reviews cite this structure
Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes.
Dougherty et al. (1993)
14 more
99 other articles
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See Also

References

  1. ↑ Pearl L, Blundell T. The active site of aspartic proteinases. FEBS Lett. 1984 Aug 20;174(1):96-101. PMID:6381096

Contents


PDB ID 4ape

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OCA

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