Structural and biochemical evidence for disulfide bond heterogeneity in active forms of the somatomedin B domain of human vitronectin. Determined by solution NMR. Released 27 Jul 2004.
Explore 1SSU in 3D Show helices and sheets RCSB PDB PDBe
1SSU contains 2 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 25-27 | 3 | |
| α-helix | 35-38 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vitronectin | A | protein | 51 | Homo sapiens | P04004 (AlphaFold model) |
>1SSU_1 Vitronectin (chains A) DQESCKGRCTEGFNVDKKCQCDELCSYYQSCCTDYTAECKPQVTRGDVFTM
Disulfide bonding arrangements in active forms of the somatomedin B domain of human vitronectin. Kamikubo, Y., De Guzman, R., Kroon, G. et al. Biochemistry (2004) 43:6519-6534. DOI 10.1021/bi049647c · PubMed
Other PDB entries of the same protein (UniProt P04004 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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