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Crystal structure of an endo-beta-N-acetylglucosaminidase (BT_3987) from bacteroides thetaiotaomicron vpi-5482 at 1.55 a resolution

Analyse Crystal structure of an endo-beta-N-acetylglucosaminidase (BT_3987) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3POH
Type: protein
Length: 435 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-beta-N-acetylglucosaminidase F1
UniProt: Q8A0N4
Pockets: 4 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-beta-N-acetylglucosaminidase F1	protein	435	25% helix, 31% strand	Q8A0N4

Ligands and binding sites

IMD · Imidazole · additive · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	582	0.76	0.83	47	empty
2	300	0.65	0.81	42	empty
3	190	0.55	0.79	21	IMD
4	85	0.36	0.75	18	empty

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

3POH · Crystal structure of an endo-beta-N-acetylglucosaminidase (BT_3987) from BACTEROIDES… · 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 Q8A0N4
Elsewhere: RCSB PDB 3POH · PDBe 3POH · UniProt Q8A0N4

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