1ssu Summary


Structural and biochemical evidence for disulfide bond heterogeneity in active forms of the somatomedin B domain of human vitronectin

The structure was published by Kamikubo, Y., De Guzman, R., Kroon, G., et al., Scheraga, H.A., Loskutoff, D.J., and Dyson, H.J., in 2004 in a paper entitled "Disulfide bonding arrangements in active forms of the somatomedin B domain of human vitronectin." (abstract).

The structure was determined using NMR spectroscopy and deposited in 2004.

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

The PDB entry contains the structure of Vitronectin. This molecule has the UniProt identifier P04004 (VTNC_HUMAN)search. The sample contained 51 residues which is < 90% of the natural sequence. Out of 51 residues 51 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 Vitronectin P04004 (20-70) (VTNC_HUMAN)search Homo sapienssearch < 90% 51 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P04004 (20 - 70) Vitronectin Homo sapiens

Chain Structural classification (SCOP) Sequence family (Pfam)
A Somatomedin B domainsearch Somatomedin B domainsearch

Chain ID Molecular function (GO) Biological process (GO)
A (P04004) scavenger receptor activitysearch polysaccharide bindingsearch immune responsesearch

Chain InterPro annotation
A Somatomedin B domainsearch Somatomedin B, chordatasearch