MolNFT v1 · #70491 · protein

Crystal structure of a putative glycoside HYDROLASE/DEACETYLASE (BDI_3119) from parabacteroides distasonis at 1.44 a resolution

3LM3 · Uncharacterized protein: “Crystal structure of a putative glycoside HYDROLASE/DEACETYLASE (BDI_3119) from parabacteroides distasonis at…”. X-ray diffraction, 1 pocket (best druggability 0.68). MolNFT v1 #70491 on GenesisL1: 3D…

PDB: 3LM3
Type: protein
Length: 434 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: A6LGL1
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	434	37% helix, 21% strand	A6LGL1

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · 3 copies · 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	364	0.68	0.81	32	empty

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

3LM3 · Crystal structure of a putative glycoside hydrolase/deacetylase (bdi_3119) from… · 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 A6LGL1
Elsewhere: RCSB PDB 3LM3 · PDBe 3LM3 · UniProt A6LGL1

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