1mmc Summary

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1H NMR STUDY OF THE SOLUTION STRUCTURE OF AC-AMP2

The structure was published by Martins, J.C., Maes, D., Loris, R., et al., Wyns, L., Willem, R., and Verheyden, P., in 1996 in a paper entitled "H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus." (abstract).

The structure was determined using NMR spectroscopy and deposited in 1995.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of ANTIMICROBIAL PEPTIDE 2. This molecule has the UniProt identifier P27275 (AMP_AMACA)search. The sample contained 30 residues which is < 90% of the natural sequence. Out of 30 residues 30 were observed and are deposited in the PDB.

The molecule is most likely monomeric.

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 ANTIMICROBIAL PEPTIDE 2 P27275 (26-55) (AMP_AMACA)search Amaranthus caudatussearch < 90% 30 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P27275 (26 - 55) ANTIMICROBIAL PEPTIDE 2 Amaranthus caudatus

Chain Structural classification (SCOP) Sequence family (Pfam)
A Antimicrobial peptide 2, AC-AMP2search Chitin recognition proteinsearch

Chain ID Molecular function (GO)
A (P27275) chitin bindingsearch

Chain InterPro annotation
A Chitin-binding, type 1search Chitin-binding, type 1, conserved sitesearch