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First crystal structure of endo-levanase BT1760 from bacteroides thetaiotaomicron

Analyse First crystal structure of endo-levanase BT1760 from bacteroides… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6R3R
Type: protein
Length: 492 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoside hydrolase family 32
UniProt: Q8A6W6
Ligands: ZN, CL
Pockets: 3 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycoside hydrolase family 32	protein	492	5% helix, 50% strand	Q8A6W6

Ligands and binding sites

ZN · Zinc ion · metal · chains A
CL · Chloride ion · ion · 2 copies · chains A
GOL · Glycerol · additive · 9 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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	277	0.61	0.79	27	GOL
2	156	0.47	0.77	20	MES, GOL
3	64	0.28	0.73	22	empty

Compared structures

6R3R · First crystal structure of endo-levanase BT1760 from Bacteroides thetaiotaomicron · 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 Q8A6W6
Elsewhere: RCSB PDB 6R3R · PDBe 6R3R · UniProt Q8A6W6

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