Research workbench
Structure of the lactophage P2 receptor binding protein in complex with glycerol
Analyse Structure of the lactophage P2 receptor binding protein in complex with glycerol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZRU
- Type
- protein
- Length
- 758 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lactophage P2 receptor binding protein
- UniProt
- Q71AW2
- Pockets
- 5 · best druggability 0.83
Structure
x-ray diffraction · 3 distinct chains · 6% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lactophage P2 receptor binding protein | protein | 253 | 6% helix, 52% strand | Q71AW2 |
| B | Lactophage P2 receptor binding protein | protein | 251 | 6% helix, 52% strand | Q71AW2 |
| C | Lactophage P2 receptor binding protein | protein | 254 | 6% helix, 52% strand | Q71AW2 |
Ligands and binding sites
- GOL · Glycerol · additive · 6 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 334 | 0.83 | 0.92 | 28 | empty |
| 2 | 187 | 0.62 | 0.83 | 30 | GOL |
| 3 | 193 | 0.53 | 0.78 | 23 | GOL |
| 4 | 178 | 0.51 | 0.78 | 30 | GOL |
| 5 | 65 | 0.44 | 0.82 | 19 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2252 Ų buried · 44 hydrogen bonds · protein-protein
- A–C · 2202 Ų buried · 44 hydrogen bonds · protein-protein
- B–C · 2180 Ų buried · 44 hydrogen bonds · protein-protein
Compared structures
- 1ZRU · structure of the lactophage p2 receptor binding protein in complex with glycerol · 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 Q71AW2
- Elsewhere: RCSB PDB 1ZRU · PDBe 1ZRU · UniProt Q71AW2
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