MolNFT v1 · #15314 · protein
Crystal structure of phl P 1, a major timothy grass pollen allergen
1N10 · Pollen allergen phl P 1: “Crystal structure of phl P 1, a major timothy grass pollen allergen”. X-ray diffraction, 1 ligand (NAG), 7 pockets (best druggability 0.75). MolNFT v1 #15314 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1N10
- Type
- protein
- Length
- 456 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pollen allergen phl P 1
- UniProt
- P43213
- Ligands
- NAG
- Pockets
- 7 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Pollen allergen phl P 1 | protein | 228 | 7% helix, 38% strand | P43213 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 101 | 0.75 | 0.96 | 29 | empty |
| 2 | 94 | 0.75 | 0.96 | 28 | empty |
| 3 | 117 | 0.59 | 0.86 | 28 | empty |
| 4 | 169 | 0.49 | 0.77 | 30 | empty |
| 5 | 151 | 0.47 | 0.77 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 1444 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 1N10 · Crystal Structure of Phl p 1, a Major Timothy Grass Pollen Allergen · the same entry in another collection · chain A against A, TM-score 1.00
- P43213 · AlphaFold monomer V2.0 prediction for pollen allergen phl P 1 (P43213) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P43213
- Elsewhere: RCSB PDB 1N10 · PDBe 1N10 · UniProt P43213
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