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MALTOSE/MALTODEXTRIN-binding domain male from bdellovibrio bacteriovorus bound to maltotriose

Analyse MALTOSE/MALTODEXTRIN-binding domain male from bdellovibrio bacteriovorus bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6FFL
Type: protein
Length: 383 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MALTOSE/MALTODEXTRIN transport permease homologue
UniProt: Q6MNM0
Ligands: GLC, PT, SO4
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	MALTOSE/MALTODEXTRIN transport permease homologue	protein	383	46% helix, 19% strand	Q6MNM0

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 3 copies · chains A
PT · Platinum (II) ion · metal · 5 copies · chains A
SO4 · Sulfate ion · ion · chains A

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

Pockets

2 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	282	0.74	0.87	34	GLC, SO4
2	56	0.33	0.77	16	empty

Compared structures

6FFL · Maltose/maltodextrin-binding domain MalE from Bdellovibrio bacteriovorus bound to… · 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 Q6MNM0
Elsewhere: RCSB PDB 6FFL · PDBe 6FFL · UniProt Q6MNM0

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