MolNFT v1 · #61046 · protein
Crystal structure of a cleaved form of a chimeric receptor binding protein from lactococcal phages subspecies TP901-1 and P2
3DA0 · Cleaved chimeric receptor binding protein from…: “Crystal structure of a cleaved form of a chimeric receptor binding protein from lactococcal phages subspecies…”. X-ray diffraction, 1 pocket (best druggability 0.79). MolNFT v1…
- PDB
- 3DA0
- Type
- protein
- Length
- 400 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cleaved chimeric receptor binding protein from bacteriophages TP901-1 and P2
- UniProt
- Q9G096, Q71AW2
- Pockets
- 1 · best druggability 0.79
Structure
x-ray diffraction · 3 distinct chains · 2% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cleaved chimeric receptor binding protein from bacteriophages TP901-1 and P2 | protein | 132 | 2% helix, 52% strand | Q9G096, Q71AW2 |
| B | Cleaved chimeric receptor binding protein from bacteriophages TP901-1 and P2 | protein | 135 | 2% helix, 51% strand | Q9G096, Q71AW2 |
| C | Cleaved chimeric receptor binding protein from bacteriophages TP901-1 and P2 | protein | 133 | 2% helix, 52% strand | Q9G096, Q71AW2 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 294 | 0.79 | 0.90 | 31 | empty |
Interfaces
3 interfaces between chains.
- B–C · 2119 Ų buried · 49 hydrogen bonds · protein-protein
- A–C · 1971 Ų buried · 46 hydrogen bonds · protein-protein
- A–B · 1964 Ų buried · 43 hydrogen bonds · protein-protein
Compared structures
- 3DA0 · Crystal structure of a cleaved form of a chimeric receptor binding protein from… · 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 Q9G096
- Every structure of UniProt Q71AW2
- Elsewhere: RCSB PDB 3DA0 · PDBe 3DA0 · UniProt Q9G096 · UniProt Q71AW2
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