Research workbench
A common fold for the receptor binding domains of lactococcal phages? the crystal structure of the head domain of phage BIL170
Analyse A common fold for the receptor binding domains of lactococcal phages? the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FSD
- Type
- protein
- Length
- 220 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative baseplate protein
- UniProt
- O80120
- Pockets
- 2 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Putative baseplate protein | protein | 110 | 3% helix, 59% strand | O80120 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 197 | 0.49 | 0.76 | 38 | empty |
| 2 | 173 | 0.45 | 0.75 | 35 | empty |
Interfaces
1 interface between chains.
- A–B · 499 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 2FSD · A Common Fold for the Receptor Binding Domains of Lactococcal Phages? The Crystal… · 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 O80120
- Elsewhere: RCSB PDB 2FSD · PDBe 2FSD · UniProt O80120
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