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Crystal structures of the gach receptor of streptomyces glaucescens GLA.O in the unliganded form and in complex with acarbose and an acarbose homolog. comparison with acarbose-loaded maltose binding protein of salmonella typhimurium.

Analyse Crystal structures of the gach receptor of streptomyces glaucescens GLA.O in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3K02
Type: protein
Length: 388 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ACARBOSE/MALTOSE binding protein gach
UniProt: B0B0V1
Ligands: TXT, SO4
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ACARBOSE/MALTOSE binding protein gach	protein	388	48% helix, 18% strand	B0B0V1

Ligands and binding sites

TXT · 4,6-dideoxy-4-{[(1S,2R,3R,4S,5S)-2,3,4-trihydroxy-5-(hydroxymethyl)cyclohexyl]amino}-alpha-D-allopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranose · ligand · chains A
SO4 · Sulfate ion · ion · 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	452	0.72	0.82	44	TXT

Compared structures

3K02 · Crystal structures of the GacH receptor of Streptomyces glaucescens GLA.O in the… · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt B0B0V1
Elsewhere: RCSB PDB 3K02 · PDBe 3K02 · UniProt B0B0V1

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