MolNFT v1 · #98922 · protein

HA17-HA33-lac

4LO2 · Ha-33: “HA17-HA33-lac”. X-ray diffraction, 2 ligands (BGC, GAL), 6 pockets (best druggability 0.49). MolNFT v1 #98922 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4LO2
Type: protein
Length: 716 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ha-33; Ha-17
UniProt: Q45871, Q45878
Ligands: BGC, GAL
Pockets: 6 · best druggability 0.49

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ha-33	protein	286	10% helix, 47% strand	Q45871
C	Ha-17	protein	144	6% helix, 49% strand	Q45878

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 2 copies · chains A, B
GAL · beta-D-galactopyranose · sugar · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	177	0.49	0.77	28	empty
2	122	0.43	0.77	20	empty
3	77	0.43	0.80	20	empty
4	58	0.39	0.80	12	empty
5	94	0.35	0.74	17	empty

Interfaces

3 interfaces between chains.

A–B · 1003 Å² buried · 13 hydrogen bonds · protein-protein
C–B · 709 Å² buried · 7 hydrogen bonds · protein-protein
A–C · 445 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

4LO2 · HA17-HA33-Lac · 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 Q45871
Every structure of UniProt Q45878
Elsewhere: RCSB PDB 4LO2 · PDBe 4LO2 · UniProt Q45871 · UniProt Q45878

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