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C2 crystal form of mite allergen der P 1

Analyse C2 crystal form of mite allergen der P 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3F5V
Type: protein
Length: 444 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Der P 1 allergen
EC: 3.4.22.65
UniProt: Q3HWZ5
Ligands: CA
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Der P 1 allergen (EC 3.4.22.65)	protein	222	28% helix, 25% strand	Q3HWZ5

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A, B
P6G · Hexaethylene glycol · additive · 5 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	639	0.71	0.78	64	P6G

Interfaces

1 interface between chains.

A–B · 660 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 2 modified (disulfide, oxidation).

Compared structures

3F5V · C2 Crystal form of mite allergen DER P 1 · 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 Q3HWZ5
Elsewhere: RCSB PDB 3F5V · PDBe 3F5V · UniProt Q3HWZ5

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