MolNFT v1 · #114485 · protein

Crystal structure of HA17-HA33-lactulose

5BQU · Ha-33: “Crystal structure of HA17-HA33-lactulose”. X-ray diffraction, 2 ligands (FRU, GAL), 9 pockets (best druggability 0.51). MolNFT v1 #114485 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5BQU
Type: protein
Length: 706 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ha-33; Ha-17
UniProt: Q45871, Q45878
Ligands: FRU, GAL
Pockets: 9 · best druggability 0.51

Structure

x-ray diffraction · 3 distinct chains · 8% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Ha-33	protein	277	9% helix, 47% strand	Q45871
A	Ha-33	protein	285	9% helix, 47% strand	Q45871
C	Ha-17	protein	144	6% helix, 49% strand	Q45878

Ligands and binding sites

FRU · beta-D-fructofuranose · sugar · 2 copies · chains A
GAL · beta-D-galactopyranose · sugar · 2 copies · chains B, A

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

Pockets

9 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	189	0.51	0.78	28	empty
2	107	0.42	0.78	20	empty
3	74	0.42	0.80	19	empty
4	109	0.38	0.74	17	empty
5	62	0.37	0.78	14	empty

Interfaces

3 interfaces between chains.

B–A · 999 Å² buried · 15 hydrogen bonds · protein-protein
B–C · 715 Å² buried · 8 hydrogen bonds · protein-protein
A–C · 445 Å² buried · 4 hydrogen bonds · protein-protein

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 Q45871
Every structure of UniProt Q45878
Elsewhere: RCSB PDB 5BQU · PDBe 5BQU · UniProt Q45871 · UniProt Q45878

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