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Maltotetraose bound T. maritima MALE1

Analyse Maltotetraose bound T. maritima MALE1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6DTU
Type: protein
Length: 749 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Maltose-binding protein MALE1
UniProt: Q9X0T1
Ligands: GLC
Pockets: 5 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Maltose-binding protein MALE1	protein	375	49% helix, 22% strand	Q9X0T1
B	Maltose-binding protein MALE1	protein	374	49% helix, 21% strand	Q9X0T1

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 8 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1091	0.78	0.80	96	empty
2	311	0.71	0.84	32	GLC
3	399	0.69	0.81	32	GLC
4	239	0.53	0.76	37	empty
5	183	0.48	0.76	36	empty

Interfaces

1 interface between chains.

A–B · 639 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6DTU · Maltotetraose bound T. maritima MalE1 · 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 Q9X0T1
Elsewhere: RCSB PDB 6DTU · PDBe 6DTU · UniProt Q9X0T1

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