Research workbench
Native tailspike protein of bacteriophage SF6
Analyse Native tailspike protein of bacteriophage SF6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VBK
- Type
- protein
- Length
- 511 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tailspike-protein
- UniProt
- Q9XJP3
- Ligands
- MG, PO4, CO2
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tailspike-protein | protein | 511 | 8% helix, 45% strand | Q9XJP3 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A
- PO4 · Phosphate ion · ion · 3 copies · chains A
- CO2 · Carbon dioxide · ion · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 12 copies · chains A
- GOL · Glycerol · additive · 6 copies · chains A
- PGR · R-1,2-propanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2VBK · Native tailspike protein of bacteriophage SF6 · 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 Q9XJP3
- Elsewhere: RCSB PDB 2VBK · PDBe 2VBK · UniProt Q9XJP3
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