MolNFT v1 · #165965 · protein
The structure of the streptococcus gordonii surface protein sspb in complex with tev peptide provides clues to the adherence of oral streptococcal adherence to salivary agglutinin
6UBV: “The structure of the streptococcus gordonii surface protein sspb in complex with tev peptide provides clues…”. X-ray diffraction, 4 ligands (SNZ, CA, NA). MolNFT v1 #165965 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6UBV
- Type
- protein
- Length
- 1,573 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- C9E3B4
- Ligands
- SNZ, CA, NA, SO4
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 392 | — | C9E3B4 |
| B | — | protein | 394 | — | C9E3B4 |
| C | — | protein | 399 | — | C9E3B4 |
| D | — | protein | 388 | — | C9E3B4 |
Ligands and binding sites
- SNZ · N-(3,4-dihydroxyphenyl)-N'-[2-(3,4-dihydroxyphenyl) ethyl]urea · ligand · 4 copies · chains A, B, C, D
- CA · Calcium ion · metal · 4 copies · chains A, B, C, D
- NA · Sodium ion · metal · 3 copies · chains A, C, D
- SO4 · Sulfate ion · ion · 2 copies · chains A, B, C, D
- EDO · 1,2-ethanediol · additive · 3 copies · chains B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6UBV · The structure of the Streptococcus gordonii surface protein SspB in complex with TEV… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt C9E3B4
- Elsewhere: RCSB PDB 6UBV · PDBe 6UBV · UniProt C9E3B4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.