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Crystal structure of the recombinant allergen ves V 2

Analyse Crystal structure of the recombinant allergen ves V 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ATM
Type: protein
Length: 324 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hyaluronoglucosaminidase
EC: 3.2.1.35
UniProt: P49370
Ligands: SO4
Pockets: 2 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hyaluronoglucosaminidase (EC 3.2.1.35)	protein	324	48% helix, 17% strand	P49370

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	179	0.47	0.76	23	empty
2	54	0.26	0.73	12	MES

Modifications

Observed in the structure: 2 disulfide, 1 modified (disulfide, nonstandard).

Compared structures

2ATM · Crystal structure of the recombinant allergen Ves v 2 · the same entry in another collection · chain A against A, TM-score 1.00
P49370 · AlphaFold monomer V2.0 prediction for hyaluronidase a (P49370) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P49370
Elsewhere: RCSB PDB 2ATM · PDBe 2ATM · UniProt P49370

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