1a7f Summary

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INSULIN MUTANT B16 GLU, B24 GLY, DES-B30, NMR, 20 STRUCTURES

The structure was published by Ludvigsen, S., Olsen, H.B., and Kaarsholm, N.C., in 1998 in a paper entitled "A structural switch in a mutant insulin exposes key residues for receptor binding." (abstract).

The structure was determined using NMR spectroscopy and deposited in 1998.

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

This PDB entry contains a complex of 2 biomacromolecules, namely INSULIN.

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 INSULIN P01308 (90-110) (INS_HUMAN)search Homo sapienssearch 100% 21 100%
B INSULIN P01308 (25-53) (INS_HUMAN)search Homo sapienssearch 100% 29 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P01308 (90 - 110) INSULIN Homo sapiens

Chain Structural classification (SCOP) Sequence family (Pfam)
A (P01308) Insulin-likesearch PF00049: Insulin/IGF/Relaxin familysearch
B (P01308) Insulin-likesearch PF00049: Insulin/IGF/Relaxin familysearch

Chain ID Cellular component (GO) Molecular function (GO)
A (P01308) extracellular regionsearch hormone activitysearch
B (P01308) extracellular regionsearch hormone activitysearch

Chain InterPro annotation
A Insulin-likesearch Insulin, conserved sitesearch
B Insulin-likesearch