Research workbench

Ogoga apostructure

Analyse Ogoga apostructure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2XSA
Type: protein
Length: 443 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hyaluronoglucosaminidase
EC: 3.2.1.52
UniProt: Q2CEE3
Ligands: CL
Pockets: 4 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hyaluronoglucosaminidase (EC 3.2.1.52)	protein	443	47% helix, 11% strand	Q2CEE3

Ligands and binding sites

CL · Chloride ion · ion · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	53	0.61	0.93	21	empty
2	225	0.57	0.79	39	empty
3	54	0.35	0.79	14	empty
4	50	0.30	0.77	16	empty

Compared structures

2XSA · OgOGA apostructure · the same entry in another collection · chain A against A, TM-score 1.00
Q2CEE3 · AlphaFold monomer V2.0 prediction for protein O-glcnacase (Q2CEE3) · 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 Q2CEE3
Elsewhere: RCSB PDB 2XSA · PDBe 2XSA · UniProt Q2CEE3

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