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Maltotetraose bound T. maritima MALE2

Analyse Maltotetraose bound T. maritima MALE2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6DTS
Type: protein
Length: 757 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Maltose-binding protein MALE2
UniProt: Q9S5Y1
Ligands: GLC
Pockets: 5 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Maltose-binding protein MALE2	protein	379	48% helix, 20% strand	Q9S5Y1
B	Maltose-binding protein MALE2	protein	378	49% helix, 20% strand	Q9S5Y1

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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	397	0.66	0.79	43	GLC
2	377	0.64	0.78	43	GLC
3	198	0.51	0.77	32	empty
4	129	0.44	0.77	23	empty
5	80	0.36	0.76	18	empty

Interfaces

1 interface between chains.

A–B · 133 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

6DTS · Maltotetraose bound T. maritima MalE2 · 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 Q9S5Y1
Elsewhere: RCSB PDB 6DTS · PDBe 6DTS · UniProt Q9S5Y1

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