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Crystal structures and biochemical characterization of the bacterial solute receptor acbh reveal an unprecedented exclusive substrate preference for B-D-galactopyranose

Analyse Crystal structures and biochemical characterization of the bacterial solute… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3OO7
Type: protein
Length: 388 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ABC transporter binding protein acbh
UniProt: Q27GR2
Ligands: SO4
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ABC transporter binding protein acbh	protein	388	51% helix, 15% strand	Q27GR2

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A
GOL · Glycerol · additive · 6 copies · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	386	0.59	0.76	37	GOL
2	50	0.51	0.88	20	empty
3	104	0.49	0.81	22	GOL

Compared structures

3OO7 · Crystal structures and biochemical characterization of the bacterial solute receptor AcbH… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q27GR2
Elsewhere: RCSB PDB 3OO7 · PDBe 3OO7 · UniProt Q27GR2

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