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X-ray crystal structure of xenopus laevis galectin-va

Analyse X-ray crystal structure of xenopus laevis galectin-va in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WUC
Type: protein
Length: 272 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Galectin
UniProt: Q91786
Ligands: GLC, GAL
Pockets: 4 · best druggability 0.33

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 63% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Galectin	protein	135	0% helix, 64% strand	Q91786
B	Galectin	protein	137	0% helix, 63% strand	Q91786

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A, B
GAL · beta-D-galactopyranose · sugar · 2 copies · chains A, B
MLA · Malonic acid · additive · 4 copies · chains A, B

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

Pockets

4 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	58	0.33	0.77	12	empty
2	58	0.32	0.76	13	empty
3	59	0.32	0.76	19	GAL, MLA
4	84	0.32	0.73	19	GAL, MLA

Interfaces

1 interface between chains.

A–B · 612 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

3WUC · X-ray crystal structure of Xenopus laevis galectin-Va · 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 Q91786
Elsewhere: RCSB PDB 3WUC · PDBe 3WUC · UniProt Q91786

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