Research workbench

Crystal structure of putative glycosyl hydrolase (NP_813087.1) from bacteroides thetaiotaomicron vpi-5482 at 1.80 a resolution

Analyse Crystal structure of putative glycosyl hydrolase (NP_813087.1) from bacteroides… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3K11
Type: protein
Length: 439 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative glycosyl hydrolase
UniProt: Q8A045
Pockets: 1 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative glycosyl hydrolase	protein	439	53% helix, 8% strand	Q8A045

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 19 copies · 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

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	188	0.52	0.78	20	empty

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

3K11 · Crystal structure of Putative glycosyl hydrolase (NP_813087.1) 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 Q8A045
Elsewhere: RCSB PDB 3K11 · PDBe 3K11 · UniProt Q8A045

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.