Research workbench
The receptor-binding protein P2 of bacteriophage PRD1: crystal form I
Analyse The receptor-binding protein P2 of bacteriophage PRD1: crystal form I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1N7U
- Type
- protein
- Length
- 554 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adsorption protein P2
- UniProt
- P27378
- Ligands
- CA
- Pockets
- 2 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adsorption protein P2 | protein | 554 | 9% helix, 46% strand | P27378 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 104 | 0.37 | 0.75 | 24 | ACT |
| 2 | 80 | 0.36 | 0.76 | 19 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1N7U · The receptor-binding protein P2 of bacteriophage PRD1: crystal form I · 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 P27378
- Elsewhere: RCSB PDB 1N7U · PDBe 1N7U · UniProt P27378
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