1gzy Summary



The structure was published by Brzozowski, A.M., Dodson, E.J., Dodson, G.G., et al., Turkenburg, J.P., De Bree, F.M., and Dauter, Z., in 2002 in a paper entitled "Structural Origins of the Functional Divergence of Human Insulin-Like Growth Factor-I and Insulin" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.54 Å and deposited in 2002.

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

The PDB entry contains the structure of INSULIN-LIKE GROWTH FACTOR I. This molecule has the UniProt identifier P05019 (IGF1_HUMAN)search. The sample contained 70 residues which is < 90% of the natural sequence. Out of 70 residues 57 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

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
B INSULIN-LIKE GROWTH FACTOR I P05019 (49-118) (IGF1_HUMAN)search Homo sapienssearch < 90% 70 81%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P05019 (49 - 118) INSULIN-LIKE GROWTH FACTOR I Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
B Insulin-likesearch Insulin-like, subunit Esearch Insulin/IGF/Relaxin familysearch

Chain ID Cellular component (GO) Molecular function (GO)
B (P05019) extracellular spacesearch extracellular regionsearch hormone activitysearch growth factor activitysearch

Chain InterPro annotation
B Insulin-likesearch Insulin-like growth factor Isearch Insulin-like growth factorsearch Insulin familysearch Insulin, conserved sitesearch