1pip Summary

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CRYSTAL STRUCTURE OF PAPAIN-SUCCINYL-GLN-VAL-VAL-ALA-ALA-P-NITROANILIDE COMPLEX AT 1.7 ANGSTROMS RESOLUTION: NONCOVALENT BINDING MODE OF A COMMON SEQUENCE OF ENDOGENOUS THIOL PROTEASE INHIBITORS

The structure was published by Yamamoto, A., Tomoo, K., Doi, M., et al., Tsuboi, S., Okamoto, H., and Okada, Y., in 1992 in a paper entitled "Crystal structure of papain-succinyl-Gln-Val-Val-Ala-Ala-p-nitroanilide complex at 1.7-A resolution: noncovalent binding mode of a common sequence of endogenous thiol protease inhibitors." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 1992.

The experimental data on which the structure is based was not deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely PAPAIN and SUCCINYL-GLN-VAL-VAL-ALA-ALA-P-NITROANILIDE.

The molecule most likely forms heterodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A PAPAIN P00784 (134-345) (PAPA1_CARPA)search Carica papayasearch 98% 212 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00784 (134 - 345) PAPAIN Carica papaya

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P00784) Papain-likesearch Cysteine proteinasessearch PF00112: Papain family cysteine proteasesearch

Chain ID Molecular function (GO) Biological process (GO)
A (P00784) cysteine-type peptidase activitysearch proteolysissearch

Chain InterPro annotation
A Cysteine peptidase, cysteine active sitesearch Peptidase C1A, papain C-terminalsearch Peptidase C1Asearch Cysteine peptidase, histidine active sitesearch Cysteine peptidase, asparagine active sitesearch