Research workbench

Phl P 6 fold stabilized mutant - S46Y

Analyse Phl P 6 fold stabilized mutant - S46Y in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6TRK
Type: protein
Length: 215 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pollen allergen phl P 6
UniProt: P43215
Ligands: ZN
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 2 distinct chains · 80% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pollen allergen phl P 6	protein	108	81% helix, 0% strand	P43215
B	Pollen allergen phl P 6	protein	107	78% helix, 0% strand	P43215

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	85	0.35	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 770 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

6TRK · Phl p 6 fold stabilized mutant - S46Y · the same entry in another collection · chain A against A, TM-score 1.00
P43215 · AlphaFold monomer V2.0 prediction for pollen allergen phl P 6 (P43215) · a predicted model of the same protein · chain B against A, TM-score 0.90

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 P43215
Elsewhere: RCSB PDB 6TRK · PDBe 6TRK · UniProt P43215

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